// ID ACEA_ASHGO STANDARD; PRT; 560 AA. AC O94198; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ICL1. OS Ashbya gossypii (Eremothecium gossypii). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Eremotheciaceae; Eremothecium. OX NCBI_TaxID=33169; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 10895; RX MEDLINE=99154744; PubMed=10037140; RA Maeting I., Schmidt G., Sahm H., Revuelta J.L., Stierhof Y.D., RA Stahmann K.-P.; RT "Isocitrate lyase of Ashbya gossypii -- transcriptional regulation and RT peroxisomal localization."; RL FEBS Lett. 444:15-21(1999). CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ010727; CAB37065.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Peroxisome. FT ACT_SITE 217 217 BY SIMILARITY. FT SITE 558 560 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 560 AA; 62584 MW; 6E9FCA3A608438AD CRC64; MSPSVRDARN DLASLQQQAA AEAEDIRRWW SQPRWAGTKR VYTAEDIVKR RGTFPVVEYP SSVMADKLVE TLARHSRNGT VSQTFGVLDP VQMTQMVKYL DTIYVSGWQC SATASTSNEP GPDLADYPMD TVPNKVEHLF MAQLFHDRKQ REARLSCTTQ RELDQLGPEI DYLRPIVADA DTGHGGLTAV FKLTKMFIER GAAGIHMEDQ SSSNKKCGHM AGRCVIPVQE HISRLVTVRM CADVMHSNLV LVARTDSEAA TLLSSNIDAR DHYYIVGASN PEVTVPLIEV LDAAQQAGAS GDRLAQLEED WCKKAKLRLF HEAFADQVNA SPSIKDKAGV IAKFNSQIGP QTGASIREMR KLGRELLGQD VYFDWDLPRA REGLYRYKGG TQCAIMRARA FAPYADLVWF ESNFPDFQQA KEFAQGVREK FPNKWMAYNL SPSFNWPKAM PPKEQENYIQ RLGEIGYVWQ FITLAGLHTN ALAIDNFSRE FSRFGMRAYA QGIQQREMDE GVDVLKHQKW AGAEYVDSIL KLAQGGVSST ASMGKGVTEE QFGSSNGAKL // ID ACEA_CANAL STANDARD; PRT; 550 AA. AC Q9P8Q7; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ICL1. OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP SEQUENCE FROM N.A. RA Eschrich D., Koetter P., Entian K.; RT "Gluconeogenesis of Candida albicans."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF222905; AAF34690.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Peroxisome. FT ACT_SITE 210 210 PROBABLE. FT SITE 548 550 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 550 AA; 61394 MW; FFBDB59FB60BE337 CRC64; MPYTPIDIQK EEADFQKEVA EIKKWWSEPR WRKTKRIYSA EDIAKKRGTL KINHPSSQQA DKLFKLLETH DADKTVSFTF GALDPIHVAQ MAKYLDSIYV SGWQCSSTAS TSNEPSPDLA DYPMDTVPNK VEHLWFAQLF HDRKQREERL TLSKEERAKT PYIDFLRPII ADADTGHGGI TAIIKLTKMF IERGAAGIHI EDQAPGTKKC GHMAGKVLVP VQEHINRLVA IRASADIFGS NLLAVARTDS EAATLITSTI DHRDHYFIIG ATNPEAGDLA ALMAEAESKG IYGNELAAIE SEWTKKAGLK LFHEAVIDEI KNGNYSNKDA LIKKFTDKVN PLSHTSHKEA KKLAKELTGK DIYFNWDVAR AREGYYRYQG GTQCAVMRGR AFAPYADLIW MESALPDYAQ AKEFADGVKA AVPDQWLAYN LSPSFNWNKA MPADEQETYI KRLGKLGYVW QFITLAGLHT TALAVDDFSN QYSQIGMKAY GQTVQQPEIE KGVEVVKHQK WSGATYIDGL LKMVSGGVTS TAAMGQGVTE DQFKESKAKA // ID ACEA_CANTR STANDARD; PRT; 550 AA. AC P20014; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ICL1. OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5482; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90299863; PubMed=2361956; RA Atomi H., Ueda M., Hikida M., Hishida T., Teranishi Y., Tanaka A.; RT "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast RT Candida tropicalis: gene analysis and characterization."; RL J. Biochem. 107:262-266(1990). CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D00703; BAA00611.1; -. DR PIR; JX0105; WZCKI. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Peroxisome. FT ACT_SITE 210 210 PROBABLE. FT SITE 548 550 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 550 AA; 61576 MW; BA86F18169B5AC0C CRC64; MAYTKIDINQ EEADFQKEVA EIKKWWSEPR WRKTKRIYSA EDIAKKRGTL KIAYPSSQQS DKLFKLLEKH DAEKSVSFTF GALDPIHVAQ MAKYLDSIYV SGWQCSSTAS TSNEPSPDLA DYPMDTVPNK VEHLWFAQLF HDRKQREERL NMTKEERANT PYIDFLRPII ADADTGHGGI TAIIKLTKLF IERGAAGIHI EDQAPGTKKC GHMAGKVLVP VQEHINRLVA IRASADIFGS NLLAVARTDS EAATLITSTI DHRDHYFIIG ATNPESGDLA ALMAEAEAKG IYGDELARIE TEWTKKAGLK LFHEAVIDEI KAGNYSNKEA LIKKFTDKVN PLSHTSHKEA KKLAKELTGK DIYFNWDVAR AREGYYRYQG GTQCAVMRGR AFAPYADLIW MESALPDYNQ AKEFADGVKA AVPDQWLAYN LSPSFNWNKA MPADEQETYI KRLGQLGYVW QFITLAGLHT TALAVDDFAN QYSQIGMRAY GQTVQQPEIE KGVEVVKHQK WSGANYIDGL LRMVSGGVTS TAAMGAGVTE DQFKETKAKV // ID ADAS_CAEEL STANDARD; PRT; 597 AA. AC O45218; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) (Alkyl-DHAP DE synthase) (Alkylglycerone-phosphate synthase). OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98113342; PubMed=9446784; RA de Vet E.C.J.M., Prinsen H.C.M.T., van den Bosch H.; RT "Nucleotide sequence of a cDNA clone encoding a Caenorhabditis elegans RT homolog of mammalian alkyl-dihydroxyacetonephosphate synthase: RT evolutionary switching of peroxisomal targeting signals."; RL Biochem. Biophys. Res. Commun. 242:277-281(1998). CC -!- CATALYTIC ACTIVITY: 1-ACYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN CC ALCOHOL = 1-ALKYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN ACID ANION. CC -!- COFACTOR: FAD (BY SIMILARITY). CC -!- PATHWAY: ETHER LIPID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE FAD-BINDING OXIDOREDUCTASE/TRANSFERASE CC FAMILY 4. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ002686; CAA05690.1; -. DR InterPro; IPR001575; Oxid_FAD_bind. DR Pfam; PF01565; FAD_binding_4; 1. KW Lipid synthesis; Transferase; Flavoprotein; FAD; Peroxisome. FT SITE 595 597 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 597 AA; 66559 MW; 6224D6A11E0811AB CRC64; MSASYQTIEH DVPQSYRDKI LKWNGWGYSD SQFAINKDGH VTFTGDKYEI SGKVMPHFRP WFENYLGIDL GFVSPAQKLS DVIIDAPVEN EDIIEFLQEN KISFSNEARI RLMRGHGHTV HDMINLREGK IPRLPDIVVW PKSEHEIVKI IEGAMSHNCA IIPIGGGTSV TNALDTPETE KRAVISMDMA LLDKILWIDR ENLTCRAQAG IVGQSLERQL NKKGFTCGHE PDSIEFSTLG GWVSTRASGM KKNKYGNIED LVVHLNFVCP KGIIQKQCQV PRMSSGPDIH QIILGSEGTL GVVSEVTIKI FPIPEVKRFG SFVFPNFESG VNFFREVAIQ RCQPASLRLM DNDQFVMGQA LKVASDSWWA DLKSSVSKMY ITSWKGFKVD EICAATCVYE GNREEVDQHE ERLNKLAEQF HGVVGGAENG QYGYRLTFAI AYLRDLGMNH GVLGESFETS VPWDKVLSLC RNVKELMKRE AKAQGVTHPV LANCRVTQVY DAGACVYFYF GFNARGLKNG LEVYDRIETA ARDEIIACGG SISHHHGVGK IRKQWMLTTN GAVGIALLKA IKSELDPANI FASANLIDII GSPHCKL // ID ADAS_DICDI STANDARD; PRT; 611 AA. AC O96759; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) (Alkyl-DHAP DE synthase) (Alkylglycerone-phosphate synthase). OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=KASSX-3; RX MEDLINE=99057552; PubMed=9837757; RA de Vet E.C.J.M., van den Bosch H.; RT "Nucleotide sequence of alkyl-dihydroxyacetonephosphate synthase cDNA RT from Dictyostelium discoideum."; RL Biochem. Biophys. Res. Commun. 252:629-633(1998). CC -!- CATALYTIC ACTIVITY: 1-ACYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN CC ALCOHOL = 1-ALKYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN ACID ANION. CC -!- COFACTOR: FAD (BY SIMILARITY). CC -!- PATHWAY: ETHER LIPID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE FAD-BINDING OXIDOREDUCTASE/TRANSFERASE CC FAMILY 4. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ010740; CAA09333.1; -. DR DictyDb; DD0????; -. DR InterPro; IPR001575; Oxid_FAD_bind. DR Pfam; PF01565; FAD_binding_4; 1. KW Lipid synthesis; Transferase; Flavoprotein; FAD; Peroxisome. FT SITE 609 611 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 611 AA; 69407 MW; 99B1221683350271 CRC64; MSGEKKEYPK EHIDLYQQIK WNGWGDTRKF LHQLKPSGTI AMTTPEVSSV PLPSLRGFIK KELTLPGEED KPFVLDETPA LQIENIHVDP PKQYPEFVRE LKAFFLPDQL KDDKLARITH TFGKSLRDLI RVRIGQVKNA PDLIVLPHSH EEVERLVQLA HKYNVVIIPM GGGSNIVGAI EPVSNERFTV SIDMRRMNKV LWVDRREMTA CIQVGIMGPE LEKQLHKQGV SLGHDPDSFE FSTLGGWLAT CSSGHQSDKY GDIEDMAVSF RTVTPTGTLE LRNGARSGAG INYKHIILGS EGTLGIITEA VMKVHAVPQA VEYYGFLFPT FAHAVSALQQ IRSSEVIPTM IRVYDPEETQ LSFAWKPSKG AVSEFTSAMV KKYLHYIRSF DFKNVCLSII GFEGPKKVVD FHRTSVFDIL SKNAAFGLGS APGKTWAEKR YDLPYIRDFL LDHNMWVDVA ETTVSYANLQ TLWKDAKQTF VKHFKDQGIP AWICAHISHT YTNGVCLYFI FASKQNENKD MAQYIEAKKL MTDIIFKYGG SLSHHHGVGY EHVPWMTRYA TRGWINVYRS LKETIDPKDI CNPRKLIPTI KEENNKEPFL FDVVNVKYPK L // ID ADAS_DROME STANDARD; PRT; 631 AA. AC Q9V778; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) (Alkyl-DHAP DE synthase) (Alkylglycerone-phosphate synthase). GN CG10253. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: 1-ACYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN CC ALCOHOL = 1-ALKYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN ACID ANION. CC -!- COFACTOR: FAD (BY SIMILARITY). CC -!- PATHWAY: ETHER LIPID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FAD-BINDING OXIDOREDUCTASE/TRANSFERASE CC FAMILY 4. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE003812; AAF58181.1; -. DR FlyBase; FBgn0033983; CG10253. DR InterPro; IPR001575; Oxid_FAD_bind. DR Pfam; PF01565; FAD_binding_4; 1. KW Lipid synthesis; Transferase; Flavoprotein; FAD; Peroxisome. FT SITE 629 631 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 631 AA; 70821 MW; AEDD6FDDA6BFB862 CRC64; MAAKRNAVTT EAPESSAPGE GTALALDSRL SKRVESVIPK KRHEALKWFG WGYNDSQFYG KDGIICFRGE KYPLGGCELP SFTKWVEKKF DLRVDTTKQY PQLPRTYPRP VENAPFLHEL KGTTQVDYSA EGIDRLVRCH GQTLNDIYSL WHHKFRRIPD LVVWPRCHDE VVQLVRLANK HNVMLVPFGG GTSVSGAITC PQNESRMICA LDTSQMNRLL WLNRENLTVC FESGIVGQDL ERVLRSEGLT VGHEPDSYEF STLGGWVATR ASGMKKNVYG NIEDLVVRVR MVTPSGTLER ECSAPRVSCG PDFNHVILGS EGTLGVITEV VLKVRPLPSL RRYGSLAFPN FEQGVLFMRE VARRRCQPAS VRLMDNEQFM FGQALKPEKS WWASVVDAMK QRYVTSWKGI DLNQICAATL LFEGDLKDVQ RQEALIYEIA EKFQGFPAGG QNGERGYILT FVIAYIRDFG LHQGIVAESF ETSVPWDRCS LLCRSVKQRV VSECSKRSIN YYTISCRVTQ TYDAGACIYF YFGFRSTDVA DPVELFEAIE HSARDEILSC GGSLSHHHGV GKIRSHWYRN AVTETGSSLY SAAKRHLDPK NIFALGNLLP LEEAQASPPP PTSSTPPKAK L // ID ADAS_TRYBB STANDARD; PRT; 613 AA. AC O97157; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alkyldihydroxyacetonephosphate synthase (EC 2.5.1.26) (Alkyl-DHAP DE synthase) (Alkylglycerone-phosphate synthase). OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP SEQUENCE FROM N.A. RA Zomer A.M.W., Michels P.A.M., Opperdoes F.R.; RT "Molecular characterization of Trypanosoma brucei alkyl- RT dihydroxyacetonephosphate synthase."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 1-ACYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN CC ALCOHOL = 1-ALKYL-GLYCERONE 3-PHOSPHATE + A LONG-CHAIN ACID ANION. CC -!- COFACTOR: FAD (BY SIMILARITY). CC -!- PATHWAY: ETHER LIPID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FAD-BINDING OXIDOREDUCTASE/TRANSFERASE CC FAMILY 4. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF119091; AAD19697.1; -. DR InterPro; IPR001575; Oxid_FAD_bind. DR Pfam; PF01565; FAD_binding_4; 1. KW Lipid synthesis; Transferase; Flavoprotein; FAD; Peroxisome. FT SITE 611 613 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 613 AA; 69067 MW; 27BA9FBF2EB94E3A CRC64; MDKRMITDAF EEIKWNGWGD TGVCIKYDEA RQLPIHTNGK PMKHLLKFMK DDVLKVKGEF KIKPTPGLTK EEAIKRLPPP VVKQPFVDEL RQVLSKDQIR LDAYARLTHI FGKNYRDLWR VRRGMIDRPP DAVILPNNHD DCVKIMELAQ KHNVVVVPFG GGTNVTGGVE PNPFETRRMV ISIDMRRMGR MLHIDTESGT AVFEVGVLGP DIDEQLSRYG FMMGHDPDSY AYSTLGGWIA ARGSGAMSNK YGDIENMILA MRVVTPVGVV ETPLTSRPCG VDLNAMFVGS EGAFGLVTEA VVKIERLPEV KRYEGWLFPS FEVAFTAFHT CTRKGIHPCT MRLYDEDDTR LSFAASTDSG LVSTFFSKCF KKYIATVKGW NLSKISLVVV GFEGTKAQTN CQRSELVGVF QAFGATCLGT KPGNTWQEKK YDLPYLRDFA LAHNFWADVF ETSVLYTDAI HCWRAVKKSF AEVMAENGKN AWIGCHTAHQ YRFGCCLYFT FIGGQADEND LKIFLQVKKR AMEVMLQHRG NLTHHHGIGY EHVPWMKRYN GEGGLDAIMK FKKALDPKNI CNPGKLLPSP PSEKETPKAT QARQNREMMF DKMGIPGALQ AHL // ID AHP1_YEAST STANDARD; PRT; 176 AA. AC P38013; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal alkyl hydroperoxide reductase (EC 1.6.4.-). GN AHP1 OR YLR109W OR L2916 OR L9354.5. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FY23 / RD005; RA Verhasselt P., Volckaert G.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., RA Favello A., Fulton L., Gattung S., Greco T., Kirsten J., Kucaba T., RA Hallsworth K., Hawkins J., Hillier L., Jier M., Johnson D., RA Johnston L., Langston Y., Latreille P., Le T., Mardis E., Menezes S., RA Miller N., Nhan M., Pauley A., Peluso D., Rifken L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 82-99. RC STRAIN=S288C; RX MEDLINE=95203288; PubMed=7895733; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein RT database."; RL Electrophoresis 15:1466-1486(1994). RN [4] RP CHARACTERIZATION. RX MEDLINE=99143107; PubMed=9988687; RA Lee J., Spector D., Godon C., Labarre J., Toledano M.B.; RT "A new antioxidant with alkyl hydroperoxide defense properties in RT yeast."; RL J. Biol. Chem. 274:4537-4544(1999). RN [5] RP CHARACTERIZATION. RX MEDLINE=20101469; PubMed=10635552; RA Farcasanu I.C., Hirata D., Tsuchiya E., Mizuta K., Miyakawa T.; RT "Involvement of thioredoxin peroxidase type II (Ahp1p) of RT Saccharomyces cerevisiae in Mn2+ homeostasis."; RL Biosci. Biotechnol. Biochem. 63:1871-1881(1999). CC -!- FUNCTION: ANTIOXIDANT PROTEIN WITH ALKYL HYDROPEROXIDASE ACTIVITY. CC SPECIFIC FOR ORGANIC PEROXIDES. INVOLVED IN CELLULAR MN2+ CC HOMEOSTASIS. CC -!- SUBUNIT: HOMODIMER; DISULFIDE-LINKED, UPON OXIDATION. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PEROXIREDOXIN 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X89514; CAA61687.1; -. DR EMBL; Z73281; CAA97676.1; -. DR EMBL; U53878; AAB67554.1; -. DR COMPLUYEAST-2DPAGE; P38013; -. DR YEPD; 9212; -. DR SGD; S0007480; AHP1. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Peroxidase; Membrane; Peroxisome. FT SITE 174 176 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). SQ SEQUENCE 176 AA; 19115 MW; 11B730781306A015 CRC64; MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI ITGAPAAFSP TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW AKSLGVKDTT HIKFASDPGC AFTKSIGFEL AVGDGVYWSG RWAMVVENGI VTYAAKETNP GTDVTVSSVE SVLAHL // ID ALOX_CANBO STANDARD; PRT; 663 AA. AC Q00922; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-OCT-1993 (Rel. 27, Last annotation update) DE Alcohol oxidase (EC 1.1.3.13) (AOX) (Methanol oxidase) (MOX). GN AOD1. OS Candida boidinii (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5477; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 2-11; 13-18 AND 20-35. RC STRAIN=S2; RX MEDLINE=92267386; PubMed=1587486; RA Sakai Y., Tani Y.; RT "Cloning and sequencing of the alcohol oxidase-encoding gene (AOD1) RT from the formaldehyde-producing asporogeneous methylotrophic yeast, RT Candida boidinii S2."; RL Gene 114:67-73(1992). CC -!- CATALYTIC ACTIVITY: PRIMARY ALCOHOL + O(2) = ALDEHYDE + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- PATHWAY: IT IS THE FIRST REACTION IN C1-METABOLISM IN YEAST CC WHEREIN METHANOL IS OXIDIZED TO FORMALDEHYDE, WHICH IS THEN CC BROKEN DOWN TO CARBON DIOXIDE. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE GMC OXIDOREDUCTASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81702; AAA34321.1; -. DR PIR; JC1117; JC1117. DR InterPro; IPR000172; GMC_oxred. DR Pfam; PF00732; GMC_oxred; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. KW Oxidoreductase; Flavoprotein; FAD; Methanol utilization; Peroxisome. FT NP_BIND 8 39 FAD (ADP PART) (BY SIMILARITY). FT SITE 661 663 MICROBODY TARGETING SIGNAL FT (BY SIMILARITY). SQ SEQUENCE 663 AA; 74082 MW; BC2E2F595B326AA6 CRC64; MAIPEEFDVI VCGGGSTGCV IAGRLANVDE NLKVLLIENG ENNLNNPWVY LPGIYPRNMR LDSKTATFYN SRPSKHLNGR RAIVPQANIL GGGSSINFMM YTRASASDYD DWESEGWTTD ELLPLMKKFE TYQRPCNNRD VHGFDGPIKV SFGNYTYPQC QDFLRACETQ GIPYVDDLED LKTSHGAEQW LKWINRDFGR RSDTAHAFIH STMRNKENLF LMTNTKVDKV IIEDGRAVAV RTVPSKPIGD SKVSRTFKAR KQIVVSCGTV SSPMVLQRSG IGEPSKLRAA GVKPIVELPG VGRNFQDHFC YFVPYRIKQD SESFDAFVSG DKEAQKSAFD QWYATGAGPL ATNGIEAGVK IRPTEAELAT ADKAFQQGWE SYFENKPDKP LMHYSVISGF FGDHTRLPPG KYMTMFHFLE YPFSRGWLHI SSDDPYAAPD FDPGFMNDDR DMWPMVWAFK KSRETARRME CFAGEPTAFH PHYKVDSPAR ALEQSAEDTK KVAGPLHLTA NLYHGSWSTP IGEADKHDPN HVTSSHINVY SKDIQYTKED DEAIENYIKE HAETTWHCLG TNSMAPREGN KNAPEGGVLD PRLNVHGVKG LKVADLSVCP DNVGCNTFST ALTIGEKAAV LVAEDLGYSG SELDMEVPQH KLKTYEQTGA ARY // ID ALOX_PICAN STANDARD; PRT; 664 AA. AC P04841; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Alcohol oxidase (EC 1.1.3.13) (AOX) (Methanol oxidase) (MOX). GN MOX. OS Pichia angusta (Yeast) (Hansenula polymorpha). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4905; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85215671; PubMed=2582370; RA Ledeboer A.M., Edens L., Maat J., Visser C., Bos J.W., Verrips C.T.; RT "Molecular cloning and characterization of a gene coding for methanol RT oxidase in Hansenula polymorpha."; RL Nucleic Acids Res. 13:3063-3082(1985). RN [2] RP SIMILARITY TO DROSOPHILA GLUCOSE DEHYDROGENASE. RX MEDLINE=91163320; PubMed=2002763; RA Cavener D.R., Krasney P.; RT "Drosophila glucose dehydrogenase and yeast alcohol oxidase are RT homologous and share N-terminal homology with other flavoenzymes."; RL Mol. Biol. Evol. 8:144-150(1991). RN [3] RP REVIEW. RX MEDLINE=91353074; PubMed=1882546; RA van der Klei I.J., Harder W., Veenhuis M.; RT "Biosynthesis and assembly of alcohol oxidase, a peroxisomal matrix RT protein in methylotrophic yeasts: a review."; RL Yeast 7:195-209(1991). CC -!- CATALYTIC ACTIVITY: PRIMARY ALCOHOL + O(2) = ALDEHYDE + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- PATHWAY: IT IS THE FIRST REACTION IN C1-METABOLISM IN YEAST CC WHEREIN METHANOL IS OXIDIZED TO FORMALDEHYDE, WHICH IS THEN CC BROKEN DOWN TO CARBON DIOXIDE. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE GMC OXIDOREDUCTASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02425; CAA26278.1; -. DR EMBL; A11156; CAA00941.1; -. DR PIR; A23010; OXHQAP. DR InterPro; IPR000172; GMC_oxred. DR Pfam; PF00732; GMC_oxred; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. KW Oxidoreductase; Flavoprotein; FAD; Methanol utilization; Peroxisome. FT NP_BIND 8 39 FAD (ADP PART) (PROBABLE). FT ACT_SITE 573 573 POTENTIAL. FT SITE 662 664 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 664 AA; 74089 MW; 6A4E3AFD6688BD5D CRC64; MAIPDEFDII VVGGGSTGCC IAGRLANLDD QNLTVALIEG GENNINNPWV YLPGVYPRNM RLDSKTATFY SSRPSKALNG RRAIVPCANI LGGGSSINFL MYTRASASDY DDWESEGWST DELLPLIKKI ETYQRPCNNR DLHGFDGPIK VSFGNYTYPT CQDFLRAAES QGIPVVDDLE DFKTSHGAEH WLKWINRDLG RRSDSAHAYV HPTMRNKQSL FLITSTKCDK VIIEDGKAVA VRTVPMKPLN PKKPVSRTFR ARKQIVISCG TISSPLVLQR SGIGAAHHLR SVGVKPIVDL PGVGENFQDH YCFFTPYYVK PDVPTFDDFV RGDPVAQKAA FDQWYSNKDG PLTTNGIEAG VKIRPTEEEL ATADEDFRRG YAEYFENKPD KPLMHYSVIS GFFGDHTKIP NGKFMTMFHF LEYPFSRGFV RITSANPYDA PDFDPGFLND ERDLWPMVWA YKKSRETARR MESFAGEVTS HHPLFKVDSP ARARDLDLET CSAYAGPKHL TANLYHGSWT VPIDKPTPKN DFHVTSNQVQ LHSDIEYTEE DDEAIVNYIK EHTETTWHCL GTCSMAPREG SKIAPKGGVL DARLNVYGVQ NLKVADLSVC PDNVGCNTYS TALTIGEKAA TLVAEDLGYS GSDLDMTIPN FRLGTYEETG LARF // ID AMAC_HUMAN STANDARD; PRT; 382 AA. AC Q9UHK6; O43673; Q9Y3Q1; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA DE racemase). GN AMACR. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND VARIANTS M-9; P-52; P-107; D-175; L-201;E-277. RX MEDLINE=20120722; PubMed=10655068; RA Ferdinandusse S., Denis S., Clayton P.T., Graham A., Rees J.E., RA Allen J.T., McLean B.N., Brown A.Y., Vreken P., Waterham H.R., RA Wanders R.J.A.; RT "Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA RT racemase cause adult-onset sensory motor neuropathy."; RL Nat. Genet. 24:188-191(2000). RN [2] RP SEQUENCE FROM N.A. RA Albers C., Schmitz W., Conzelmann E.; RT "Human alpha-methylacyl-CoA racemase cDNA sequence."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A., SUBCELLULAR LOCATION, AND MICROBODY TARGETING. RX MEDLINE=20515663; PubMed=11060344; RA Amery L., Fransen M., De Nys K., Mannaerts G.P., Van Veldhoven P.P.; RT "Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase RT in humans."; RL J. Lipid Res. 41:1752-1759(2000). RN [4] RP CHARACTERIZATION. RC TISSUE=Liver; RX MEDLINE=95377317; PubMed=7649182; RA Schmitz W., Albers C., Fingerhut R., Conzelmann E.; RT "Purification and characterization of an alpha-methylacyl-CoA racemase RT from human liver."; RL Eur. J. Biochem. 231:815-822(1995). CC -!- FUNCTION: RACEMIZATION OF 2-METHYL-BRANCHED FATTY ACID COA ESTERS. CC RESPONSIBLE FOR THE CONVERSION OF PRISTANOYL-COA AND C27-BILE CC ACYL-COAS TO THEIR (S)-STEREOISOMERS. CC -!- CATALYTIC ACTIVITY: (2S)-2-METHYLACYL-COA = (2R)-2-METHYLACYL-COA. CC -!- PATHWAY: REQUIRED FOR BILE ACID SYNTHESIS AND FOR CATABOLISM OF CC BRANCHED-CHAIN FATTY ACIDS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL AND MITOCHONDRIAL. CC -!- DISEASE: DEFECTS IN AMACR RESULT IN A FORM OF ADULT ONSET SENSORY CC MOTOR NEUROPATHY. IT IS CAUSED BY ELEVATED CONCENTRATIONS OF CC PRISTANIC ACID. CC -!- SIMILARITY: TO BILE ACID-INDUCIBLE OPERON PROTEIN F (BAIF) FROM CC EUBACTERIUM SP. AND TO E.COLI CAIB. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A CC FRAMESHIFT IN POSITION 62-144. THE FIGURE IN THE PAPER IS CORRECT, CC BUT THE SEQUENCE SUBMISSION IS INCORRECT. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF158378; AAF22610.1; -. DR EMBL; AF047020; AAD10205.1; -. DR EMBL; AJ130733; CAB44062.1; ALT_FRAME. DR MIM; 604489; -. DR InterPro; IPR003673; CAIB_BAIF. DR Pfam; PF02515; CAIB-BAIF; 1. KW Isomerase; Peroxisome; Mitochondrion; Polymorphism; Disease mutation. FT SITE 379 382 MICROBODY TARGETING SIGNAL. FT VARIANT 9 9 V -> M. FT /FTId=VAR_010660. FT VARIANT 52 52 S -> P (IN AMACR DEFICIENCY). FT /FTId=VAR_010661. FT VARIANT 107 107 L -> P (IN AMACR DEFICIENCY). FT /FTId=VAR_010665. FT VARIANT 175 175 G -> D. FT /FTId=VAR_010662. FT VARIANT 201 201 S -> L. FT /FTId=VAR_010663. FT VARIANT 277 277 K -> E. FT /FTId=VAR_010664. FT CONFLICT 18 18 P -> R (IN REF. 3). FT CONFLICT 150 150 L -> V (IN REF. 3). FT CONFLICT 183 183 N -> D (IN REF. 2). FT CONFLICT 257 257 N -> S (IN REF. 2). FT CONFLICT 261 261 M -> T (IN REF. 2 AND 3). FT CONFLICT 327 327 P -> L (IN REF. 3). FT CONFLICT 340 342 FKR -> SKG (IN REF. 3). SQ SEQUENCE 382 AA; 42359 MW; B1573CF9682E6EFD CRC64; MALQGISVVE LSGLAPGPFC AMVLADFGAR VVRVDRPGSR YDVSRLGRGK RSLVLDLKQP RGAAVLRRLC KRSDVLLEPF RRGVMEKLQL GPEILQRENP RLIYARLSGF GQSGSFCRLA GHDINYLALS GVLSKIGRSG ENPYAPLNLL ADFAGGGLMC ALGIIMALFD RTRTGKGQVI DANMVEGTAY LSSFLWKTQK SSLWEAPRGQ NMLDGGAPFY TTYRTADGEF MAVGAIEPQF YELLIKGLGL KSDELPNQMS MDDWPEMKKK FADVFAKKTK AEWCQIFDGT DACVTPVLTF EEVVHHDHNK ERGSFITSEE QDVSPRPAPL LLNTPAIPSF KRDPFIGEHT EEILEEFGFS REEIYQLNSD KIIESNKVKA SL // ID AMAC_MOUSE STANDARD; PRT; 380 AA. AC O09174; Q9DCW6; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA DE racemase). GN AMACR OR MACR1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE OF 14-380 FROM N.A. RC TISSUE=Liver; RX MEDLINE=97439733; PubMed=9307041; RA Schmitz W., Helander H.M., Hiltunen J.K., Conzelmann E.; RT "Molecular cloning of cDNA species for rat and mouse liver alpha- RT methylacyl-CoA racemases."; RL Biochem. J. 326:883-889(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX MEDLINE=21085660; PubMed=11217851; RA Kawai J., Shinagawa A., Shibata K., Yoshino M., Itoh M., Ishii Y., RA Arakawa T., Hara A., Fukunishi Y., Konno H., Adachi J., Fukuda S., RA Aizawa K., Izawa M., Nishi K., Kiyosawa H., Kondo S., Yamanaka I., RA Saito T., Okazaki Y., Gojobori T., Bono H., Kasukawa T., Saito R., RA Kadota K., Matsuda H.A., Ashburner M., Batalov S., Casavant T., RA Fleischmann W., Gaasterland T., Gissi C., King B., Kochiwa H., RA Kuehl P., Lewis S., Matsuo Y., Nikaido I., Pesole G., Quackenbush J., RA Schriml L.M., Staubli F., Suzuki R., Tomita M., Wagner L., Washio T., RA Sakai K., Okido T., Furuno M., Aono H., Baldarelli R., Barsh G., RA Blake J., Boffelli D., Bojunga N., Carninci P., de Bonaldo M.F., RA Brownstein M.J., Bult C., Fletcher C., Fujita M., Gariboldi M., RA Gustincich S., Hill D., Hofmann M., Hume D.A., Kamiya M., Lee N.H., RA Lyons P., Marchionni L., Mashima J., Mazzarelli J., Mombaerts P., RA Nordone P., Ring B., Ringwald M., Rodriguez I., Sakamoto N., RA Sasaki H., Sato K., Schoenbach C., Seya T., Shibata Y., Storch K.-F., RA Suzuki H., Toyo-oka K., Wang K.H., Weitz C., Whittaker C., Wilming L., RA Wynshaw-Boris A., Yoshida K., Hasegawa Y., Kawaji H., Kohtsuki S., RA Hayashizaki Y.; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [3] RP SEQUENCE OF 1-15, PARTIAL SEQUENCE FROM N.A., & SUBCELLULAR LOCATION. RX MEDLINE=20347188; PubMed=10770938; RA Kotti T.J., Savolainen K., Helander H.M., Yagi A., Novikov D.K., RA Kalkkinen N., Conzelmann E., Hiltunen J.K., Schmitz W.; RT "In mouse alpha-methylacyl-CoA racemase, the same gene product is RT simultaneously located in mitochondria and peroxisomes."; RL J. Biol. Chem. 275:20887-20895(2000). CC -!- FUNCTION: RACEMIZATION OF 2-METHYL-BRANCHED FATTY ACID COA ESTERS. CC RESPONSIBLE FOR THE CONVERSION OF PRISTANOYL-COA AND C27-BILE CC ACYL-COAS TO THEIR (S)-STEREOISOMERS. CC -!- CATALYTIC ACTIVITY: (2S)-2-METHYLACYL-COA = (2R)-2-METHYLACYL-COA. CC -!- PATHWAY: REQUIRED FOR BILE ACID SYNTHESIS AND FOR CATABOLISM OF CC BRANCHED-CHAIN FATTY ACIDS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL AND MITOCHONDRIAL. CC -!- SIMILARITY: TO BILE ACID-INDUCIBLE OPERON PROTEIN F (BAIF) FROM CC EUBACTERIUM SP. AND TO E.COLI CAIB. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U89906; AAB72146.1; ALT_INIT. DR EMBL; AK002401; BAB22072.1; ALT_INIT. DR MGD; MGI:1098273; Macr1. DR InterPro; IPR003673; CAIB_BAIF. DR Pfam; PF02515; CAIB-BAIF; 1. KW Isomerase; Peroxisome; Mitochondrion. FT INIT_MET 0 0 FT SITE 377 380 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). FT CONFLICT 177 177 I -> V (IN REF. 2). SQ SEQUENCE 380 AA; 41586 MW; 8BEFCE13683A3CDB CRC64; VLRGVRVVEL AGLAPGPFCG MVLADFGAEV VRVNRLGSTG ENFLARGKRS LALDLKRSQG VTVLRRMCAR ADVLLEPFRC GVMEKLQLGP ETLLQDNPKL IYARLSGFGQ SGIFSKVAGH DINYLALSGV LSKIGRSGEN PYPPLNLLAD FGGGGLMCTL GIVLALFERT RSGRGQIIDS SMVEGTAYLS SFLWKTQPMG LWKQPRGQNI LDGGAPFYTT YKTADGEFMA VGAIEPQFYA LLLKGLGLES EELPSQMSSA DWPEMKKKFA DVFAKKTKAE WCQIFDGTDA CVTPVLTFEE ALHHQHNRER ASFITDGEQL PSPRPAPLLS RTPAVPSAKR DPSVGEHTVE VLREYGFSQE EILQLHSDRI VESDKLKANL // ID AMAC_RAT STANDARD; PRT; 381 AA. AC P70473; O09176; DT 01-NOV-1997 (Rel. 35, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Alpha-methylacyl-CoA racemase (EC 5.1.99.4) (2-methylacyl-CoA DE racemase) (2-arylpropionyl-CoA epimerase). GN AMACR. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE OF 10-381 FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=97260501; PubMed=9106621; RA Reichel C., Brugger R., Bang H., Geisslinger G., Brune K.; RT "Molecular cloning and expression of a 2-arylpropionyl-coenzyme A RT epimerase: a key enzyme in the inversion metabolism of ibuprofen."; RL Mol. Pharmacol. 51:576-582(1997). RN [2] RP SEQUENCE OF 2-381 FROM N.A. RC TISSUE=Liver; RX MEDLINE=97439733; PubMed=9307041; RA Schmitz W., Helander H.M., Hiltunen J.K., Conzelmann E.; RT "Molecular cloning of cDNA species for rat and mouse liver alpha- RT methylacyl-CoA racemases."; RL Biochem. J. 326:883-889(1997). RN [3] RP PARTIAL SEQUENCE FROM N.A. RX MEDLINE=20347188; PubMed=10770938; RA Kotti T.J., Savolainen K., Helander H.M., Yagi A., Novikov D.K., RA Kalkkinen N., Conzelmann E., Hiltunen J.K., Schmitz W.; RT "In mouse alpha-methylacyl-CoA racemase, the same gene product is RT simultaneously located in mitochondria and peroxisomes."; RL J. Biol. Chem. 275:20887-20895(2000). RN [4] RP SEQUENCE OF 102-116, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX MEDLINE=96112049; PubMed=8615858; RA Reichel C., Bang H., Brune K., Geisslinger G., Menzel S.; RT "2-arylpropionyl-CoA epimerase: partial peptide sequences and tissue RT localization."; RL Biochem. Pharmacol. 50:1803-1806(1995). RN [5] RP CHARACTERIZATION. RC TISSUE=Liver; RX MEDLINE=94291625; PubMed=8020470; RA Schmitz W., Fingerhut R., Conzelmann E.; RT "Purification and properties of an alpha-methylacyl-CoA racemase from RT rat liver."; RL Eur. J. Biochem. 222:313-323(1994). CC -!- FUNCTION: RACEMIZATION OF 2-METHYL-BRANCHED FATTY ACID COA ESTERS. CC RESPONSIBLE FOR THE CONVERSION OF PRISTANOYL-COA AND C27-BILE CC ACYL-COAS TO THEIR (S)-STEREOISOMERS. HAS A ROLE IN DRUG CC METABOLISM AS WELL AS PROBABLY IN LIPID METABOLISM. THE 2- CC ARYLPROPIONIC ACID (2-APA'S) DERIVATIVES, INCLUDING IBUPROFEN, ARE CC THE MOST WIDELY USED ANTI-INFLAMMATORY ANALGESIC CYCLOOXYGENASE CC INHIBITORS. THE (-)-R-ENANTIOMER, WHICH IS INACTIVE IN TERMS OF CC CYCLOOXYGENASE INHIBITION, IS EPIMERIZED IN VIVO VIA THIS ENZYME CC TO THE CYCLOOXYGENASE-INHIBITING (+)-S-ENANTIOMER. CC -!- CATALYTIC ACTIVITY: (2S)-2-METHYLACYL-COA = (2R)-2-METHYLACYL-COA. CC -!- PATHWAY: REQUIRED FOR BILE ACID SYNTHESIS AND FOR CATABOLISM OF CC BRANCHED-CHAIN FATTY ACIDS. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL AND MITOCHONDRIAL. CC -!- SIMILARITY: TO BILE ACID-INDUCIBLE OPERON PROTEIN F (BAIF) FROM CC EUBACTERIUM SP. AND TO E.COLI CAIB. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y08172; CAA69358.1; ALT_INIT. DR EMBL; U89905; AAB72145.1; ALT_INIT. DR InterPro; IPR003673; CAIB_BAIF. DR Pfam; PF02515; CAIB-BAIF; 1. KW Isomerase; Peroxisome; Mitochondrion. FT INIT_MET 0 0 BY SIMILARITY. FT SITE 378 381 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). FT CONFLICT 69 70 CA -> FS (IN REF. 1). FT CONFLICT 79 79 F -> L (IN REF. 1). FT CONFLICT 110 110 G -> W (IN REF. 3). FT CONFLICT 165 165 L -> V (IN REF. 1). FT CONFLICT 323 323 C -> F (IN REF. 1). FT CONFLICT 327 327 A -> S (IN REF. 1). FT CONFLICT 335 335 A -> S (IN REF. 1). FT CONFLICT 339 340 AK -> SQ (IN REF. 1). SQ SEQUENCE 381 AA; 41697 MW; 2FE410CA9E453F7C CRC64; ALRGVRVLEL AGLAPGPFCG MILADFGAEV VLVDRLGSVN HPSHLARGKR SLALDLKRSP GAAVLRRMCA RADVLLEPFR CGVMEKLQLG PETLRQDNPK LIYARLSGFG QSGIFSKVAG HDINYVALSG VLSKIGRSGE NPYPPLNLLA DFGGGGLMCT LGILLALFER TRSGLGQVID ANMVEGTAYL STFLWKTQAM GLWAQPRGQN LLDGGAPFYT TYKTADGEFM AVGAIEPQFY TLLLKGLGLE SEELPSQMSI EDWPEMKKKF ADVFARKTKA EWCQIFDGTD ACVTPVLTLE EALHHQHNRE RGSFITDEEQ HACPRPAPQL SRTPAVPSAK RDPSVGEHTV EVLKDYGFSQ EEIHQLHSDR IIESNKLKAN L // ID AOFN_ASPNG STANDARD; PRT; 495 AA. AC P46882; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Monoamine oxidase N (EC 1.4.3.4) (MAO-N). GN MAON. OS Aspergillus niger. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5061; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 165-175. RX MEDLINE=95287865; PubMed=7770050; RA Schilling B., Lerch K.; RT "Cloning, sequencing and heterologous expression of the monoamine RT oxidase gene from Aspergillus niger."; RL Mol. Gen. Genet. 247:430-438(1995). CC -!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + CC H(2)O(2). CC -!- COFACTOR: FAD; NONCOVALENTLY BOUND. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (PROBABLE). CC -!- SIMILARITY: BELONGS TO THE FLAVIN MONOAMINE OXIDASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L38858; AAA98490.1; -. DR InterPro; IPR001613; Amineoxid_fl. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR001327; FAD_pyr_redox. DR Pfam; PF01593; Amino_oxidase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 40 95 FAD (ADP PART) (POTENTIAL). FT SITE 493 495 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 495 AA; 55616 MW; 0E614FF09D3C5B3D CRC64; MTSRDGYQWT PETGLTQGVP SLGVISPPTN IEDTDKDGPW DVIVIGGGYC GLTATRDLTV AGFKTLLLEA RDRIGGRSWS SNIDGYPYEM GGTWVHWHQS HVWREITRYK MHNALSPSFN FSRGVNHFQL RTNPTTSTYM THEAEDELLR SALHKFTNVD GTNGRTVLPF PHDMFYVPEF RKYDEMSYSE RIDQIRDELS LNERSSLEAF ILLCSGGTLE NSSFGEFLHW WAMSGYTYQG CMDCLISYKF KDGQSAFARR FWEEAAGTGR LGYVFGCPVR SVVNERDAAR VTARDGREFA AKRLVCTIPL NVLSTIQFSP ALSTERISAM QAGHVNMCTK VHAEVDNKDM RSWTGIAYPF NKLCYAIGDG TTPAGNTHLV CFGTDANHIQ PDEDVRETLK AVGQLAPGTF GVKRLVFHNW VKDEFAKGAW FFSRPGMVSE CLQGLREKHR GVVFANSDWA LGWRSFIDGA IEEGTRAARV VLEELGTKRE VKARL // ID AOPP_HUMAN STANDARD; PRT; 161 AA. AC P30044; Q9UBU5; Q9UKX4; Q9UJU4; DT 01-APR-1993 (Rel. 25, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Putative peroxisomal antioxidant enzyme (PLP) (TPx type VI) DE (Thioredoxin peroxidase PMP20) (Antioxidant enzyme B166) (AOEB166) DE (Liver tissue 2D-page spot 71B). GN PRDX5. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RA Kim I.H., Jeong W.; RT "A new type of human thiol peroxidase (Human TPx type VI)."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Adrenal gland; RX MEDLINE=20402571; PubMed=10931946; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [3] RP SEQUENCE FROM N.A. RA Zhou Y., Kung H.-F., Jin D.-Y.; RT "Human and mouse peroxiredoxin PMP20 is a thioredoxin peroxidase that RT inhibits p53-induced apoptosis."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Lung; RX MEDLINE=99452929; PubMed=10521424; RA Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., RA Duconseille E., Falmagne P., Bernard A.; RT "Cloning and characterization of AOEB166, a novel mammalian RT antioxidant enzyme of the peroxiredoxin family."; RL J. Biol. Chem. 274:30451-30458(1999). RN [5] RP SEQUENCE OF 1-10. RC TISSUE=Liver; RX MEDLINE=93162045; PubMed=1286669; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PEROXIREDOXIN 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ249483; CAB62210.1; -. DR EMBL; AF112212; AAF17200.1; -. DR EMBL; AF197952; AAF04856.1; ALT_INIT. DR EMBL; AF110731; AAF03750.1; ALT_INIT. DR SWISS-2DPAGE; P30044; HUMAN. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. KW Antioxidant; Peroxisome; Polymorphism. FT INIT_MET 0 0 FT SITE 159 161 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). FT VARIANT 88 88 T -> H. FT /FTId=VAR_009872. SQ SEQUENCE 161 AA; 16863 MW; F8107E18DA51146D CRC64; APIKVGDAIP AVEVFEGEPG NKVNLAELFK GKKGVLFGVP GAFTPGCSKT HLPGFVEQAE ALKAKGVQVV ACLSVNDAFV TGEWGRATKA EGKVRLLADP TGAFGKETDL LLDDSLVSIF GNRRLKRFSM VVQDGIVKAL NVEPDGTGLT CSLAPNIISQ L // ID AOPP_MOUSE STANDARD; PRT; 161 AA. AC P99029; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Putative peroxisomal antioxidant enzyme (Liver tissue 2D-page spot DE 2D-0014IV). GN PRDX5. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE OF 1-12. RC TISSUE=Liver; RA Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X., RA Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., RA Cowthorne M.; RL Submitted (AUG-1998) to the SWISS-PROT data bank. RN [2] RP SEQUENCE FROM N.A., AND RECONSTRUCTION FROM ESTS. RA Bairoch A.; RL Unpublished observations (SEP-1998). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7.6, ITS MW IS: 14.6 KDA. CC -!- SIMILARITY: BELONGS TO THE PEROXIREDOXIN 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AA589489; -; NOT_ANNOTATED_CDS. DR EMBL; AA823871; -; NOT_ANNOTATED_CDS. DR EMBL; W48365; -; NOT_ANNOTATED_CDS. DR EMBL; W71344; -; NOT_ANNOTATED_CDS. DR SWISS-2DPAGE; P99029; MOUSE. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. KW Antioxidant; Peroxisome. FT INIT_MET 0 0 FT SITE 159 161 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). FT CONFLICT 6 6 G -> D (IN REF. 1). SQ SEQUENCE 161 AA; 16883 MW; 213400E1F9487B41 CRC64; APIKVGDAIP SVEVFEGEPG KKVNLAELFK GKKGVLFGVP GAFTPGCSKT HLPGFVEQAG ALKAKGAQVV ACLSVNDVFV IEEWGRAHQA EGKVRLLADP TGAFGKATDL LLDDSLVSLF GNRRLKRFSM VIDNGIVKAL NVEPDGTGLT CSLAPNILSQ L // ID CACP_CANTR STANDARD; PRT; 627 AA. AC Q00614; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Carnitine O-acetyltransferase precursor (EC 2.3.1.7) (Carnitine DE acetylase). GN CAT2 OR CAT. OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5482; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PK233; RX MEDLINE=96300253; PubMed=8706689; RA Kawachi H., Atomi H., Ueda M., Tanaka A.; RT "Peroxisomal and mitochondrial carnitine acetyltransferases of the n- RT alkane-assimilating yeast Candida Tropicalis. Analysis of gene RT structure and translation products."; RL Eur. J. Biochem. 238:845-852(1996). CC -!- FUNCTION: CARNITINE ACETYLASE IS SPECIFIC FOR SHORT CHAIN FATTY CC ACIDS. CARNITINE ACETYLASE SEEMS TO AFFECT THE FLUX THROUGH THE CC PYRUVATE DEHYDROGENASE COMPLEX. IT MAY BE INVOLVED AS WELL IN THE CC TRANSPORT OF ACETYL-COA INTO MITOCHONDRIA (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ACETYL-COA + CARNITINE = COA + CC O-ACETYLCARNITINE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL AND IN MITOCHONDRIAL INNER CC MEMBRANE; INNER SIDE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D84549; BAA12696.1; -. DR InterPro; IPR000542; Carn_acyltransf. DR InterPro; IPR000865; Microbodies_C. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; FALSE_NEG. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; FALSE_NEG. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome; Mitochondrion; Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 627 CARNITINE O-ACETYLTRANSFERASE. FT ACT_SITE 336 336 POTENTIAL. FT SITE 625 627 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 627 AA; 70762 MW; B00878F37CC7D84B CRC64; MFNFKLSQQV LKNSTKSIMP ILKKPFSTSH AKGDLFKYQS QLPKLPVPTL EETASKYLKT VEPFLNQEQL ESTKAKVAEF VRPGGAGEAL QARLNNFAAD KDNWLAEFWD DYAYMSYRDP VVPYVSYFFS HKDVKNIIGQ DQLLKATLIA YYTIEFQEKV LDESLDPEVI KGNPFCMNAF KYMFNNSRVP AEGSDITQHY NGEENQFFVV IYKNNFYKVP THKNGQRLTK GEIYSYLQEI KNDATPKGLG LGALTSLNRD EWLSAYNNLL KSPINEASLG SIFASSFVIA LDSNNPVTIE EKSKNCWHGD GQNRFFDKPL EFFVSANGNS GFLGEHSRMD ATPTVQLNNT IYKQILETNP NDLIVEIGSS APRFGNAEIL PFDINPTTRA NIKDAIAKFD ATIAAHDEEI FQHYGYGKGL IKKFKVSPDA YVQLLMQLAY FKYTGKIRPT YESAATRKFL KGRTETGRTV SNESKKFVET WSDPNASSAD KVATFQAAAK QHVAYLSAAA DGKGVDRHLF GLKQMIQPGE PIPEIFTDPI FSYSQTWYIS SSQVPSEFFQ SWGWSQVIDD GFGLAYLINN DWIHVHISCK RGNGLQSDHL KWYLVDSANE MKDVLTKGLL TDAKPKL // ID CACP_COLLI STANDARD; PRT; 627 AA. AC P52826; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Carnitine O-acetyltransferase precursor (EC 2.3.1.7) (Carnitine DE acetylase) (CAT). OS Columba livia (Domestic pigeon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba. OX NCBI_TaxID=8932; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver, and Breast muscle; RX MEDLINE=95134223; PubMed=7832757; RA Johnson T.M., Kocher H.P., Anderson R.C., Nemecek G.M.; RT "Cloning, sequencing and heterologous expression of a cDNA encoding RT pigeon liver carnitine acetyltransferase."; RL Biochem. J. 305:439-444(1995). CC -!- FUNCTION: CARNITINE ACETYLASE IS SPECIFIC FOR SHORT CHAIN FATTY CC ACIDS. CARNITINE ACETYLASE SEEMS TO AFFECT THE FLUX THROUGH THE CC PYRUVATE DEHYDROGENASE COMPLEX. IT MAY BE INVOLVED AS WELL IN THE CC TRANSPORT OF ACETYL-COA OUT OF THE MITOCHONDRIA FOR FATTY ACID CC BIOSYNTHESIS OR URINARY EXCRETION. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + CARNITINE = COA + CC O-ACETYLCARNITINE. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM, PEROXISOMAL AND IN CC MITOCHONDRIAL INNER MEMBRANE; INNER SIDE (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08229; AAA80570.1; -. DR InterPro; IPR000542; Carn_acyltransf. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome; Mitochondrion. FT PROPEP 1 30 FT CHAIN 31 627 CARNITINE O-ACETYLTRANSFERASE. FT ACT_SITE 344 344 POTENTIAL. FT SITE 625 627 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 627 AA; 71066 MW; DD42317336AF0D2A CRC64; MDRKQKQAEK ARPYGLLKPA ALGKIPGRFQ LHQEALPHLP VPPLQQTLDR YLLALQPIIS EEELNHTQEL VAEFRKPGGV GERLQKGLER RAKKTDNWLS DWWLKTAYLE YRLPVVVHSS PGVVLPKQDF QDRQGQLRFA AKLIEGILDF KTMIDNETLP VEYMGGKPLC MNQYYQILSS CRIPGPKRDS IVNYAKGKKQ SRHITVVHNF QFFELDVYNS DGSPLTTDQL FIQLEKIWNT SLQTNKEPVG ILTTNHRNSW AKAYNNLLKD KTNKESVRTI EKSICTICLD APMPRVSDDI YKSPVAAQML HGGGSRWNSG NRWFDKTLQF IIAEDGSCGL VYEHAPAEGP PIVALLDHIV EYTKKPELVR SPMIPLPMPK KLRFNITPEI KSDIEKAKQN LNIMVEDLDV IVLVFHQFGK NYPKSEKISP DAFIQLALQL AYYRMYGHSC ATYESASLRM FRLGRTDTIR STSIESHKFV QSMDSPDKSD QEKADLLRRA TQAHKEYTNM AIQGNAIDRH LLGLKLQAIE DLVSIPELFM DTAYAVAMHF NLSTSQVPAK TDCVMCFGPV VPDGYGICYN PMGEHINFAI SAFNSCADTN AARMAHYLEK ALLDMRSLLQ SAPKSKL // ID CACP_HUMAN STANDARD; PRT; 626 AA. AC P43155; DT 01-NOV-1995 (Rel. 32, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Carnitine O-acetyltransferase (EC 2.3.1.7) (Carnitine acetylase) DE (CAT). GN CRAT OR CAT1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE OF 3-626 FROM N.A. RX MEDLINE=95130117; PubMed=7829107; RA Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.; RT "Molecular cloning of cDNAs encoding human carnitine RT acetyltransferase and mapping of the corresponding gene to chromosome RT 9q34.1."; RL Genomics 23:94-99(1994). RN [2] RP SEQUENCE OF 1-52 FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=95031982; PubMed=7945262; RA Corti O., DiDonato S., Finocchiaro G.; RT "Divergent sequences in the 5' region of cDNA suggest alternative RT splicing as a mechanism for the generation of carnitine RT acetyltransferases with different subcellular localizations."; RL Biochem. J. 303:37-41(1994). RN [3] RP PARTIAL SEQUENCE. RA Stone K., Williams K.; RL Unpublished results, cited by: RL Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.; RL Genomics 23:94-99(1994). CC -!- FUNCTION: CARNITINE ACETYLASE IS SPECIFIC FOR SHORT CHAIN FATTY CC ACIDS. CARNITINE ACETYLASE SEEMS TO AFFECT THE FLUX THROUGH THE CC PYRUVATE DEHYDROGENASE COMPLEX. IT MAY BE INVOLVED AS WELL IN THE CC TRANSPORT OF ACETYL-COA INTO MITOCHONDRIA. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + CARNITINE = COA + CC O-ACETYLCARNITINE. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM, PEROXISOMAL AND IN CC MITOCHONDRIAL INNER MEMBRANE; INNER SIDE (POTENTIAL). CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A MITOCHONDRIAL FORM (SHOWN CC HERE) AND A PEROXISOMAL FORM; SEEM TO BE PRODUCED BY ALTERNATIVE CC SPLICING. CC -!- TISSUE SPECIFICITY: MOSTLY IN SKELETAL MUSCLE, LESS IN HEART, CC LIVER, AND PANCREAS, ONLY WEAKLY DETECTABLE IN BRAIN, PLACENTA, CC LUNG, AND KIDNEY. CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78706; CAA55359.1; -. DR EMBL; X79825; -; NOT_ANNOTATED_CDS. DR MIM; 600184; -. DR InterPro; IPR000542; Carn_acyltransf. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome; Mitochondrion; Alternative splicing. FT ACT_SITE 343 343 POTENTIAL. FT SITE 624 626 MICROBODY TARGETING SIGNAL (POTENTIAL). FT VARSPLIC 1 21 MISSING (IN PEROXISOMAL ISOFORM). SQ SEQUENCE 626 AA; 70765 MW; F0F5961BA94275EB CRC64; MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE EEWAHTKQLV DEFQASGGVG ERLQKGLGRR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGFP IVTLLDYVIE YTKKPELVRS PMVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFGRHL LGLKLQAIED LVSTPDIFMD TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA ARLAHYLEKA LLDMRALLQS HPRAKL // ID CACP_MOUSE STANDARD; PRT; 627 AA. AC P47934; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Carnitine O-acetyltransferase (EC 2.3.1.7) (Carnitine acetylase) DE (CAT). GN CRAT. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97218095; PubMed=9065756; RA Brunner S., Kramar K., Denhardt D.T., Hofbauer R.; RT "Cloning and characterization of murine carnitine acetyltransferase: RT evidence for a requirement during cell cycle progression."; RL Biochem. J. 322:403-410(1997). CC -!- FUNCTION: CARNITINE ACETYLASE IS SPECIFIC FOR SHORT CHAIN FATTY CC ACIDS. CARNITINE ACETYLASE SEEMS TO AFFECT THE FLUX THROUGH THE CC PYRUVATE DEHYDROGENASE COMPLEX. IT MAY BE INVOLVED AS WELL IN THE CC TRANSPORT OF ACETYL-COA INTO MITOCHONDRIA. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + CARNITINE = COA + CC O-ACETYLCARNITINE. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM, PEROXISOMAL AND IN CC MITOCHONDRIAL INNER MEMBRANE; INNER SIDE (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X85983; CAA59971.1; -. DR MGD; MGI:109501; Crat. DR InterPro; IPR000542; Carn_acyltransf. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome; Mitochondrion. FT ACT_SITE 344 344 POTENTIAL. FT SITE 625 627 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 627 AA; 70834 MW; 15C7209A0665342A CRC64; MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDYY LKALQPIVSE EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE WWLKTAYLQL PDKPVVIYSS PGVILPKQDF VDLQGQLRFA AKLIEGVLDF KSMIDNETLP VEFLGGQPLC MNQYYQILSS CREPGPKQDS VVNFLKSKRP PTHITVVHNY QFFELDVYNS DGTPLTSDQI FVQLEKIWNS SLQSNKEPVG ILTSNHRNTW AKAYNNLIKD KVNRESVNSI QKSIFTVCLD KQVPRVSDDV YRNHVAGQML HGGGSKFNSG NRWFDKTLQF IVAEDGSCGM VYEHAAAEGP PIVALVDHVM EYTKKPELVR SPMVPLPMPK KLRFNITPEI KNDIEKAKQN LSIMIQDLDI MMLTFHHFGK DFPKSEKLSP DAFIQVALQL AYYRIYGQAC ATYESASLRM FHLGRTDTIR SASIDSLAFV KGMGDSTVPE QQKVELLRKA VQAHRAYTDR AIRGEAFDRH LLGLKLQAIE DLVSMPDIFM DTSYAIAMHF NLSTSQVPAK TDCVMFFGPV VPDGYGICYN PMEAHINLSV SAYNSCAETN AARMAHYLEK ALLDMRTLLQ NHPRAKL // ID CACP_YEAST STANDARD; PRT; 670 AA. AC P32796; DT 01-OCT-1993 (Rel. 27, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Carnitine O-acetyltransferase precursor (EC 2.3.1.7) (Carnitine DE acetylase). GN CAT2 OR CAT OR YCAT OR YML042W OR YM8054.01. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93131929; PubMed=8420957; RA Kispal G., Sumegi B., Dietmeier K., Bock I., Gajdos G., Tomcsanyi T., RA Sandor A.; RT "Cloning and sequencing of a cDNA encoding Saccharomyces cerevisiae RT carnitine acetyltransferase. Use of the cDNA in gene disruption RT studies."; RL J. Biol. Chem. 268:1824-1829(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Connor R., Churcher C., Barrell B.G., Rajandream M.A.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP ALTERNATIVE INITIATION. RX MEDLINE=95354665; PubMed=7628448; RA Elgersma Y., van Roermund C.W.T., Wanders R.J.A., Tabak H.F.; RT "Peroxisomal and mitochondrial carnitine acetyltransferases of RT Saccharomyces cerevisiae are encoded by a single gene."; RL EMBO J. 14:3472-3479(1995). CC -!- FUNCTION: CARNITINE ACETYLASE IS SPECIFIC FOR SHORT CHAIN FATTY CC ACIDS. CARNITINE ACETYLASE SEEMS TO AFFECT THE FLUX THROUGH THE CC PYRUVATE DEHYDROGENASE COMPLEX. IT MAY BE INVOLVED AS WELL IN THE CC TRANSPORT OF ACETYL-COA INTO MITOCHONDRIA. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + CARNITINE = COA + CC O-ACETYLCARNITINE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL AND IN MITOCHONDRIAL INNER CC MEMBRANE; INNER SIDE. CC -!- INDUCTION: BY ETHANOL. REPRESSED BY GALACTOSE. CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z14021; CAA78399.1; -. DR EMBL; Z48430; CAA88327.1; -. DR PIR; S28519; S28519. DR PIR; A44423; A44423. DR SGD; S0004506; CAT2. DR InterPro; IPR000542; Carn_acyltransf. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome; Mitochondrion; Transit peptide; Alternative initiation. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 670 CARNITINE O-ACETYLTRANSFERASE, FT MITOCHONDRIAL ISOFORM. FT CHAIN 23 670 CARNITINE O-ACETYLTRANSFERASE, FT PEROXISOMAL ISOFORM. FT INIT_MET 23 23 FOR PEROXISOMAL ISOFORM. FT ACT_SITE 378 378 POTENTIAL. FT SITE 668 670 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 263 263 D -> H (IN REF. 1). FT CONFLICT 308 308 L -> M (IN REF. 1). SQ SEQUENCE 670 AA; 77241 MW; C707BAC7ECB4D095 CRC64; MRICHSRTLS NLKDLPITSR RAMHSAIVNY STQKAQFPVE TNNGEHYWAE KPNKFYQNKR PNFQGITFAK QQDLPSLPVP ELKSTLDKYL QTIRPFCNDV ETFERQQLLC KDFSEHMGPI LQDRLKEYAN DKRNWMAKFW DEQSYLQYND PIVPYVSYFY SHMPLPNHLS KIDNDPLIKA TAIISTVVKF IEAIKDESLP VEIIKGMPFC MNSFSLMFNT SRLPGKPEDN QDTNIFYSVY ENNFVTIAYK GKFYKLMTHD GNDKPLSENE IWRQLYSVVF QGSQSDPKLG GIGSLTSLPR DQWREVHLEL MKDPISQDSL ETIHKSSFML CLDLDQSPVT LEEKSRNCWH GDGINRFYDK SLQFLVTGNG SSGFLAEHSK MDGTPTLFLN NYVCQQLNKL DVDDFMRKVI TPSSTVAMKP MELPFIITPK IHKAIESAQL QFKETIGEHD LRVWHYNKYG KTFIKRHGMS PDAFIQQVIQ LAVFKYLKRQ LPTYEAASTR KYFKGRTETG RSVSTASLEF VSKWQNGDVP IAEKIQALKH SAKEHSTYLK NAANGNGVDR HFFGLKNMLK SNDDQIPPLF KDPLFNYSST WLISTSQLSS EYFDGYGWSQ VNDNGFGLAY MLNNEWLHIN IVNKPAKSGA SVNRLHYYLS QAADEIFDAL ENENKRKAKL // ID CAOP_CAEEL STANDARD; PRT; 659 AA. AC P34355; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Probable acyl-coenzyme A oxidase, peroxisomal (EC 1.3.3.6) (Acyl-CoA DE oxidase) (AOX). GN C48B4.1. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RX MEDLINE=94150718; PubMed=7906398; RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., RA Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., RA Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., RA Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M., RA Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., RA Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., RA Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., RA Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., RA Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., RA Waterson R., Watson A., Weinstock L., Wilkinson-Sproat J., RA Wohldman P.; RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. RT elegans."; RL Nature 368:32-38(1994). CC -!- FUNCTION: CATALYZES THE DESATURATION OF VERY LONG CHAIN ACYL-COAS CC TO 2-TRANS-ENOYL-COAS (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ACYL-COA + O(2) = TRANS-2,3-DEHYDROACYL-COA + CC H(2)O(2) (ACTS ON COA DERIVATIVES OF FATTY ACIDS WITH CHAIN LENGTH CC FROM 8 TO 18). CC -!- COFACTOR: FAD (BY SIMILARITY). CC -!- PATHWAY: INITIAL STEP OF THE PEROXISOMAL FATTY ACID BETA-OXIDATION CC SYSTEM. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: HIGH, TO OTHER ACYL-COENZYME A OXIDASES; LOW, TO ACYL- CC COA DEHYDROGENASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z29117; CAA82376.1; -. DR PIR; S40722; S40722. DR WormPep; C48B4.1; CE00491. DR InterPro; IPR002655; ACOX. DR Pfam; PF01756; ACOX; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Hypothetical protein; Oxidoreductase; Fatty acid metabolism; KW Peroxisome; Flavoprotein; FAD. FT SITE 657 659 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 659 AA; 74714 MW; 5F0D6E92F8CAA5F8 CRC64; MPLNKLIQDG DNQDLTDERF KATFDTDALA AVFHGGEDAL KRIRELRDEV TKRWHLFDAL PGAHRTRAER MEDVSRKLKN LMESVGEFAD FTNNLDMLVI IRDVMGIEGF PLALHNLMFV PTIQNQADDE QTEWWLMDAL QGKIIGTYAQ TELGHGTNLG AIETTATYDK LTEEFIIHTP TTTATKWWPG GLGTSCTHVV LVANLIIDTK NYGLHPFFVP IRDRNSYSVM SGVRVGDIGT KMGVNCVDNG FLAFDNYRIP RRNMLMKHSK VSKEGLYTAP SHPKVGYTTM LYMRSEMIYH QAYYLAMAMA ISIRYSAVRR QGEIKPGTQE VQILDYQTQQ YRIFPGLARC FAFNTAAATV RQMTENCIKQ LSHGNSDVLA DLHALSCGLK AVVTHQASQS IDQARQACGG HGYSDASYLP TLYTCSVGAC TYEGENMVML LQLSKYLMKA AAKAEKGEEM APLVAYLVKP DITETNDKFA KMLSHFEHIA RHRVMHAYRQ MIEEEKQGIE RDYAFANHSV DWTKAARAHT KLFIARGFVK SVQEVSDEAV HDVLTTLAEL YLSYELIEMS ADLTANGYLS ESDVQQIRHQ IYDSMRKTRR NAVSIVDSFD ICDRELRSVL GRRDGHVYEN LYKWAQMSPL NERNLPHVEK YLKPMTSKL // ID CAOP_HUMAN STANDARD; PRT; 660 AA. AC Q15067; Q15068; Q12863; Q15101; Q16131; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Acyl-coenzyme A oxidase 1, peroxisomal (EC 1.3.3.6) (Palmitoyl-CoA DE oxidase) (AOX). GN ACOX1 OR ACOX. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Foreskin; RX MEDLINE=94211811; PubMed=8159712; RA Varanasi U., Chu R., Chu S., Espinosa R., Lebeau M.M., Reddy J.K.; RT "Isolation of the human peroxisomal acyl-CoA oxidase gene: RT organization, promoter analysis, and chromosomal localization."; RL Proc. Natl. Acad. Sci. U.S.A. 91:3107-3111(1994). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RA Chu R., Varanasi U., Chu S., Rao S.M., Reddy J.K.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=94314953; PubMed=8040306; RA Fourner B., Saudubray J.-M., Benichou B., Lyonnet S., Munnich A., RA Clevers H., Poll-The B.T.; RT "Large deletion of the peroxisomal acyl-CoA oxidase gene in RT pseudoneonatal adrenoleukodystrophy."; RL J. Clin. Invest. 94:526-531(1994). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=94161722; PubMed=8117268; RA Aoyama T., Tsushima K., Souri M., Kamijo T., Suzuki Y., RA Shimozawa N., Orii T., Hashimoto T.; RT "Molecular cloning and functional expression of a human peroxisomal RT acyl-coenzyme A oxidase."; RL Biochem. Biophys. Res. Commun. 198:1113-1118(1994). CC -!- FUNCTION: CATALYZES THE DESATURATION OF VERY LONG CHAIN ACYL-COAS CC TO 2-TRANS-ENOYL-COAS. CC -!- CATALYTIC ACTIVITY: ACYL-COA + O(2) = TRANS-2,3-DEHYDROACYL-COA + CC H(2)O(2) (ACTS ON COA DERIVATIVES OF FATTY ACIDS WITH CHAIN LENGTH CC FROM 8 TO 18). CC -!- COFACTOR: FAD. CC -!- PATHWAY: INITIAL STEP OF THE PEROXISOMAL FATTY ACID BETA-OXIDATION CC SYSTEM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; 1 (SHOWN HERE) AND 2; ARE CC PRODUCED BY ALTERNATIVE SPLICING. CC -!- DISEASE: DEFECTS IN ACOX1 ARE THE CAUSE OF PSEUDONEONATAL CC ADRENOLEUKODYSTROPHY. A DISEASE BIOCHEMICALLY CHARACTERIZED BY AN CC ACCUMULATION OF VERY LONG CHAIN FATTY ACIDS. CC -!- SIMILARITY: HIGH, TO OTHER ACYL-COENZYME A OXIDASES; LOW, TO ACYL- CC COA DEHYDROGENASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03268; AAA19113.1; -. DR EMBL; U03254; AAA19113.1; JOINED. DR EMBL; U03255; AAA19113.1; JOINED. DR EMBL; U03256; AAA19113.1; JOINED. DR EMBL; U03258; AAA19113.1; JOINED. DR EMBL; U03259; AAA19113.1; JOINED. DR EMBL; U03260; AAA19113.1; JOINED. DR EMBL; U03261; AAA19113.1; JOINED. DR EMBL; U03263; AAA19113.1; JOINED. DR EMBL; U03264; AAA19113.1; JOINED. DR EMBL; U03265; AAA19113.1; JOINED. DR EMBL; U03266; AAA19113.1; JOINED. DR EMBL; U03267; AAA19113.1; JOINED. DR EMBL; U03268; AAA19114.1; -. DR EMBL; U03254; AAA19114.1; JOINED. DR EMBL; U03255; AAA19114.1; JOINED. DR EMBL; U03257; AAA19114.1; JOINED. DR EMBL; U03258; AAA19114.1; JOINED. DR EMBL; U03259; AAA19114.1; JOINED. DR EMBL; U03260; AAA19114.1; JOINED. DR EMBL; U03261; AAA19114.1; JOINED. DR EMBL; U03263; AAA19114.1; JOINED. DR EMBL; U03264; AAA19114.1; JOINED. DR EMBL; U03265; AAA19114.1; JOINED. DR EMBL; U03266; AAA19114.1; JOINED. DR EMBL; U03267; AAA19114.1; JOINED. DR EMBL; U07866; AAA18595.1; -. DR EMBL; X71440; CAA50574.1; -. DR EMBL; S69189; AAB30019.2; -. DR MIM; 264470; -. DR InterPro; IPR002655; ACOX. DR Pfam; PF01756; ACOX; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Fatty acid metabolism; Peroxisome; Flavoprotein; FAD; KW Alternative splicing. FT SITE 658 660 MICROBODY TARGETING SIGNAL. FT VARSPLIC 90 131 KLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGL FT Q -> NFVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFM FT PAWNLE (IN ISOFORM 2). FT CONFLICT 27 27 P -> L (IN REF. 3). FT CONFLICT 80 80 A -> R (IN REF. 3). FT CONFLICT 119 119 Q -> E (IN REF. 4). FT CONFLICT 200 200 Y -> H (IN REF. 2). FT CONFLICT 212 213 NR -> IG (IN REF. 3 AND 4). FT CONFLICT 264 264 P -> T (IN REF. 3 AND 4). FT CONFLICT 312 312 I -> M (IN REF. 3 AND 4). FT CONFLICT 332 332 F -> L (IN REF. 2). FT CONFLICT 449 449 C -> R (IN REF. 2). FT CONFLICT 531 531 L -> C (IN REF. 3 AND 4). FT CONFLICT 534 535 GL -> VV (IN REF. 3 AND 4). FT CONFLICT 615 615 V -> A (IN REF. 3). FT CONFLICT 650 650 Y -> YH (IN REF. 4). SQ SEQUENCE 660 AA; 74501 MW; 7BE708A2FB10293D CRC64; MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED LNFLTRSQRY EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQK EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITKGKCY GLHAFIVPIR ENRTHKPLPG ITVGDIGPKF GYDEIDNGYL KMDNHRIPRE NMLMKYAQVK PDGPYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE TYHRINEGIG QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG YSHCSGLPNI YVNFTPSCTF EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP ESLTEAYKLR AARLVEIAAK NLQKEVIHRK SKEVAWNLTS VDLVRASEAH LHYGLVKLFS EKLLKIQDKA IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY KHLKSLQSKL // ID CAOP_RAT STANDARD; PRT; 661 AA. AC P07872; P11354; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Acyl-coenzyme A oxidase 1, peroxisomal (EC 1.3.3.6) (Palmitoyl-CoA DE oxidase) (AOX). GN ACOX1 OR ACOX. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87250404; PubMed=3036800; RA Miyazawa S., Hayashi H., Hijikata M., Ishii N., Furuta S., RA Kagamiyama H., Osumi T., Hashimoto T.; RT "Complete nucleotide sequence of cDNA and predicted amino acid RT sequence of rat acyl-CoA oxidase."; RL J. Biol. Chem. 262:8131-8137(1987). RN [2] RP SEQUENCE OF 1-36 FROM N.A. RX MEDLINE=87250405; PubMed=3036801; RA Osumi T., Ishii N., Miyazawa S., Hashimoto T.; RT "Isolation and structural characterization of the rat acyl-CoA RT oxidase gene."; RL J. Biol. Chem. 262:8138-8143(1987). CC -!- FUNCTION: CATALYZES THE DESATURATION OF VERY LONG CHAIN ACYL-COAS CC TO 2-TRANS-ENOYL-COAS. CC -!- CATALYTIC ACTIVITY: ACYL-COA + O(2) = TRANS-2,3-DEHYDROACYL-COA + CC H(2)O(2) (ACTS ON COA DERIVATIVES OF FATTY ACIDS WITH CHAIN LENGTH CC FROM 8 TO 18). CC -!- COFACTOR: FAD. CC -!- PATHWAY: INITIAL STEP OF THE PEROXISOMAL FATTY ACID BETA-OXIDATION CC SYSTEM. CC -!- SUBUNIT: THE ENZYME CONTAINS THREE COMPONENTS A,B AND C, THE CC LATTER TWO BEING PRODUCED FROM THE FIRST BY A PROTEOLYTIC CC CLEAVAGE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; 1 (SHOWN HERE) AND 2; ARE CC PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: HIGH, TO OTHER ACYL-COENZYME A OXIDASES; LOW, TO ACYL- CC COA DEHYDROGENASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02752; AAA40666.1; -. DR EMBL; J02753; AAA40667.1; -. DR PIR; A29328; OXRTA1. DR PIR; B29328; OXRTA2. DR InterPro; IPR002655; ACOX. DR Pfam; PF01756; ACOX; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Fatty acid metabolism; Peroxisome; Flavoprotein; FAD; KW Alternative splicing. FT CHAIN 1 661 ACYL-COA OXIDASE I PEROXISOMAL, A CHAIN. FT CHAIN 1 438 ACYL-COA OXIDASE I PEROXISOMAL, B CHAIN. FT CHAIN 439 661 ACYL-COA OXIDASE I PEROXISOMAL, C CHAIN. FT SITE 659 661 MICROBODY TARGETING SIGNAL. FT VARSPLIC 90 133 KLYLANFVEPVGLNYSMFIPTLLNQGTTAQQEKWMRPSQEL FT QII -> NSVHRGHPEPLDLHLGMFLPTLLHQATAEQQERF FT FMPAWNLEIT (IN ISOFORM 2). SQ SEQUENCE 661 AA; 74678 MW; 24B1F10DF066C29E CRC64; MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV GLNYSMFIPT LLNQGTTAQQ EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITQGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE TYLRINESIG QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF EGENTVMMLQ TARFLMKIYD QVRSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTMVDINSL EGLTEAYKLR AARLVEIAAK NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS DKLPKIQDKA VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY HKHLKPLQSK L // ID CAOQ_RAT STANDARD; PRT; 700 AA. AC Q63448; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Pristanoyl-CoA oxidase (EC 1.3.3.-). GN PRCOX. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=96314484; PubMed=8706733; RA Vanhooren J.C.T., Fransen M., de Bethune B., Baumgart E., Baes M., RA Torrekens S., van Leuven F., Mannaerts G.P., van Veldhoven P.P.; RT "Rat pristanoyl-CoA oxidase. cDNA cloning and recognition of its C- RT terminal (SQL) by the peroxisomal-targeting signal 1 receptor."; RL Eur. J. Biochem. 239:302-309(1996). CC -!- FUNCTION: OXIDIZES THE COA-ESTERS OF 2-METHYL-BRANCHED FATTY CC ACIDS. CC -!- CATALYTIC ACTIVITY: ACYL-COA + O(2) = TRANS-2,3-DEHYDROACYL-COA + CC H(2)O(2). CC -!- COFACTOR: FAD. CC -!- PATHWAY: INITIAL STEP OF THE PEROXISOMAL FATTY ACID BETA-OXIDATION CC SYSTEM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: MOST ABUNDANT IN LIVER, KIDNEY, LUNG, AND CC TESTIS. PRESENT IN ALL TISSUES TESTED. CC -!- SIMILARITY: HIGH, TO OTHER ACYL-COENZYME A OXIDASES; LOW, TO ACYL- CC COA DEHYDROGENASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95188; CAA64487.1; -. DR InterPro; IPR002655; ACOX. DR Pfam; PF01756; ACOX; 1. KW Oxidoreductase; Fatty acid metabolism; Peroxisome; Flavoprotein; FAD. FT SITE 698 700 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 700 AA; 78445 MW; DE2327CEFA7423DF CRC64; MGSSSERRDS VLWSDIPKGP LSAYRARASF NSKELMLFWD GQDVLDFKKT IFSTLENDPL FARPFGADLP LEKERELNFL RCKRVFEYGF FNAEDMLKNP LKILVLMNCL GMYDWSLANK CVLHMLVFGS TIIGSGSEHH FKYLEKIYNL EIFGCFALTE LSHGSNTKAM RTTAHYDPAT QEFILHSPDF EAAKFWVGNL GKTATHAVVF AQLYTPDGQC RGLHSFLVQI RDPKTLLPMP GVMVGDMGKK LGQNGLDNGF AMFHKVRIPR QNLLDRTGNV TSEGHYHTPF KDVRQRLGAS LGSLSSGRIS IISISVVNLK LAVIIAIRFS ATRRQFGPTD KEEIPVLEYP LQQWRLLPYL AAAYALDHFS KTIFLDLIEL QRAGKVGTTV TGRQSSGREI HALASAGKPL ASWTAQRGIQ ECREVVGGHG YLAMNRFGEL RNDNDPNCTY EGDNNVLLQQ TSNYLLSLLE HPLQDGAHFT SPLKTVNFLE AYPGILGQKF MASSKADWLD SEAPLAAYRW LVCYLLRESH QRYCQEKKSR GSDFEARNNS QVYGCRPLAL AFMELTVMQR FHEHTHSSSV PPSLRTVLGR LSMLYGLWCL SQHTALLYRG GYISGEQTGK AMEDAILMLC VQLKDDAVAL VDAIAPSDFV LGSPIGRADG ELYKNLWAAV LQQSGVLERA AWWPEFTANK SVANRLKSQL // ID CATA_DICDI STANDARD; PRT; 496 AA. AC O77229; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Catalase (EC 1.11.1.6). GN CATA OR CAT. OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AX3; RA Foote C., Alexander H., Alexander S.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: OCCURS IN ALMOST ALL AEROBICALLY RESPIRING ORGANISMS AND CC SERVES TO PROTECT CELLS FROM THE TOXIC EFFECTS OF HYDROGEN CC PEROXIDE. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: HEME GROUP (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CATALASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF090443; AAC36743.1; -. DR HSSP; P00432; 7CAT. DR DictyDb; DD0????; catA. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome. FT ACT_SITE 54 54 BY SIMILARITY. FT ACT_SITE 128 128 BY SIMILARITY. FT BINDING 338 338 PROXIMAL HEME LIGAND (BY SIMILARITY). FT SITE 494 496 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 496 AA; 55683 MW; 683318B8FBAFD2E6 CRC64; MSAPVLTTSS GSPIDNNLNS MTAGVNGPIL IQDFTLIDKL AHFDRERIPE RVVHAKGAGA HGYFEVTSSD VPKWCKAKFL NKVGKRTPIF TRFSTVGGEK GSSDSERDPR GFAVKFYTEE GNFDMVGNNT PVFFIRDPSK FPDFIHTQKR NPQTNCKDPN MFWDFLGQTP ESTHQVSILF SDRGTPKSYR HMHGFSSHTL KFVNAQGKPY WVKLHFTSET GIQNYTAEEA AKMSMNDPDS ATRDLFETIA KGGEPAWKVS IQLMEFEDAL KYRFNPFDVT KIWSHKDYPL IQIGRMVLNR NPENYFAEVE QAAFSPSHMV PGIEPSPDKM LQGRLFSYPD THRHRLGVNY QQIPVNCPFA VKGGVKNYQR DGFMAVNGNG GKGPNYQPNS FGGPEPHPEF AQHKFDVSGF AARQPYNHPN DDFVQPGDLY RLMSEDAKSR FVSNLVGHMS GVTIKEIQVR AVSNFYKADK DLGARLCKGL GIDVNDVIKF AARSNL // ID CATA_DROME STANDARD; PRT; 506 AA. AC P17336; Q9VVT1; DT 01-AUG-1990 (Rel. 15, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Catalase (EC 1.11.1.6). GN CAT OR CG6871. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96239139; PubMed=8660653; RA Orr W.C., Orr E.C., Legan S.K., Sohal R.S.; RT "Molecular analysis of the Drosophila catalase gene."; RL Arch. Biochem. Biophys. 330:251-258(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90301508; PubMed=2362827; RA Orr E.C., Bewley G.C., Orr W.C.; RT "cDNA and deduced amino acid sequence of Drosophila catalase."; RL Nucleic Acids Res. 18:3663-3663(1990). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP SEQUENCE OF 76-92. RC STRAIN=VALLECAS; TISSUE=Wing imaginal disk; RX MEDLINE=93272852; PubMed=8500545; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). CC -!- FUNCTION: OCCURS IN ALMOST ALL AEROBICALLY RESPIRING ORGANISMS AND CC SERVES TO PROTECT CELLS FROM THE TOXIC EFFECTS OF HYDROGEN CC PEROXIDE. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: HEME GROUP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE CATALASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U00145; AAC13738.1; -. DR EMBL; X52286; CAA36529.1; ALT_SEQ. DR EMBL; AE003519; AAF49228.1; -. DR PIR; S12725; CSFF. DR HSSP; P00432; 7CAT. DR FlyBase; FBgn0000261; Cat. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome. FT ACT_SITE 73 73 BY SIMILARITY. FT ACT_SITE 146 146 BY SIMILARITY. FT BINDING 356 356 PROXIMAL HEME LIGAND (BY SIMILARITY). FT SITE 504 506 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 5 5 D -> Y (IN REF. 1). FT CONFLICT 12 12 I -> N (IN REF. 1). SQ SEQUENCE 506 AA; 57149 MW; 396377DC5F784ECE CRC64; MAGRDAASNQ LIDYKNSQTV SPGAITTGNG APIGIKDASQ TVGPRGPILL QDVNFLDEMS HFDRERIPER VVHAKGAGAF GYFEVTHDIT QYCAAKIFDK VKKRTPLAVR FSTVGGESGS ADTARDPRGF AVKFYTEDGV WDLVGNNTPV FFIRDPILFP SFIHTQKRNP QTHLKDPDMF WDFLTLRPES AHQVCILFSD RGTPDGYCHM NGYGSHTFKL INAKGEPIYA KFHFKTDQGI KNLDVKTADQ LASTDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTYEQAKKF KYNPFDVTKV WSQKEYPLIP VGKMVLDRNP KNYFAEVEQI AFSPAHLVPG VEPSPDKMLH GRLFSYSDTH RHRLGPNYLQ IPVNCPYKVK IENFQRDGAM NVTDNQDGAP NYFPNSFNGP QECPRARALS SCCPVTGDVY RYSSGDTEDN FGQVTDFWVH VLDKCAKKRL VQNIAGHLSN ASQFLQERAV KNFTQVHADF GRMLTEELNL AKSSKF // ID CATA_PICAN STANDARD; PRT; 507 AA. AC P30263; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Catalase (EC 1.11.1.6). GN PXP9 OR PXP-9. OS Pichia angusta (Yeast) (Hansenula polymorpha). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4905; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 34438; RX MEDLINE=92299073; PubMed=1607006; RA Didion T., Roggenkamp R.O.; RT "Targeting signal of the peroxisomal catalase in the methylotrophic RT yeast Hansenula polymorpha."; RL FEBS Lett. 303:113-116(1992). CC -!- FUNCTION: OCCURS IN ALMOST ALL AEROBICALLY RESPIRING ORGANISMS AND CC SERVES TO PROTECT CELLS FROM THE TOXIC EFFECTS OF HYDROGEN CC PEROXIDE. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: HEME GROUP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE CATALASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56501; CAA39856.1; -. DR PIR; S23422; S23422. DR HSSP; P00432; 7CAT. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome. FT ACT_SITE 65 65 BY SIMILARITY. FT ACT_SITE 138 138 BY SIMILARITY. FT BINDING 348 348 PROXIMAL HEME LIGAND (BY SIMILARITY). FT SITE 505 507 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 507 AA; 57849 MW; 3536ED0A49539CC3 CRC64; MSNPPVFTTS QGCPVSDPFT TQRIPLDSTG YKYAPPIGPL LLQDFKLIDT LSHFDRERIP ERVVHAKGAG AYGVFEVTDD ITDVCSAKFL DTVGKKTRIF TRFSTVGGEK GSADTARDPR GFATKFYTED GNLDLVYNNT PIFFIRDPIK FPHFIHTQKR NPATNLKDPN MFWDYLTAND ESLHQVMYLF SNRGTPASYR TMNGYSGHTY KWYNSKGEWV YVQVHFIANQ GVHNLLDEEA GRLAGEDPDH STRDLWEAIE KGDYPSWECY IQTMTLEQSK KLPFSVFDLT KVWPHKDFPL RHFGRFTLNE NPKNYYAETE QIAFSPSHTV PGMEPSNDPV LQSRLFSYPD THRHRLGPNY HQIPVNCPLK SGSFNPINRD GPMCVDGNLG GTPNYANAYN CPIQYAVSPK ASGNKPDEKY TGEVVPYHWE HTDYDYFQPK MFWKVLGRTP GEQESLVKNV ANHVSAADEF IQDRVYEYFS KAEPIIGDLI RKKVQELKRK ASSPSKI // ID CATA_TOXGO STANDARD; PRT; 502 AA. AC Q9XZD5; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Catalase (EC 1.11.1.6). OS Toxoplasma gondii. OC Eukaryota; Alveolata; Apicomplexa; Coccidia; Eimeriida; Sarcocystidae; OC Toxoplasma. OX NCBI_TaxID=5811; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=RH; RA Kaasch A.J., Joiner K.A.; RT "Peroxisomes: a new organelle in the apicomplexan parasite Toxoplasma RT gondii."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=RH; RA Ding M., Clayton C., Soldati D.; RT "Toxoplasma gondii catalase: evidence for the existence of RT peroxisomes in Apicomplexa."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: OCCURS IN ALMOST ALL AEROBICALLY RESPIRING ORGANISMS AND CC SERVES TO PROTECT CELLS FROM THE TOXIC EFFECTS OF HYDROGEN CC PEROXIDE. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: HEME GROUP (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE CATALASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF136344; AAD30129.1; -. DR EMBL; AF161267; AAD45528.2; -. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome. FT ACT_SITE 64 64 BY SIMILARITY. FT ACT_SITE 137 137 BY SIMILARITY. FT BINDING 347 347 PROXIMAL HEME LIGAND (BY SIMILARITY). FT SITE 500 502 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 502 AA; 57270 MW; FBA8F0551434B74D CRC64; MTQVPPVTFQ QYGPVITTSA GNPVDDNQNS VTAGPYGPAI LSNFHLIDKL AHFDRERIPE RVVHAKGGGA FGYFEVTHDI TRFCKAKLFE KIGKRTPVFA RFSTVAGESG SADTRRDPRG FALKFYTEEG NWDMVGNNTP IFFVRDAIKF PDFIHTQKRH PQTHLHDPNM VWDFFSLVPE SVHQVTFLYT DRGTPDGFRH MNGYGSHTFK FINKDNEAFY VKWHFKTNQG IKNLNRQRAK ELESEDPDYA VRDLFNAIAK REFPSWTFCI QVMPLKDAET YKWNVFDVTK VWPHGDYPLI PVGKLVLDRN PENYFQDVEQ AAFAPAHMVP GIEPSEDRML QGRMFSYIDT HRHRLGANYH QIPVNRPWNA RGGDYSVRDG PMCVDGNKGS QLNYEPNSVD GFPKEDRNAA VSGTTTVSGT VACHPQEHPN SDFEQPGNFY RTVLSEPERE ALIGNIAEHL RQARRDIQER QVKIFYKCDP EYGERVARAI GLPTAACYPA KM // ID CATA_YEAST STANDARD; PRT; 515 AA. AC P15202; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Catalase A (EC 1.11.1.6). GN CTA1 OR YDR256C OR YD9320A.06C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88329055; PubMed=3046940; RA Cohen G., Rapatz W., Ruis H.; RT "Sequence of the Saccharomyces cerevisiae CTA1 gene and amino acid RT sequence of catalase A derived from it."; RL Eur. J. Biochem. 176:159-163(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Murphy L., Harris D., Barrell B.G., Rajandream M.A., Walsh S.V.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX MEDLINE=99134394; PubMed=9931255; RA Mate M.J., Zamocky M., Nykyri L.M., Herzog C., Alzari P.M., Betzel C., RA Koller F., Fita I.; RT "Structure of catalase-A from Saccharomyces cerevisiae."; RL J. Mol. Biol. 286:135-149(1999). CC -!- FUNCTION: OCCURS IN ALMOST ALL AEROBICALLY RESPIRING ORGANISMS AND CC SERVES TO PROTECT CELLS FROM THE TOXIC EFFECTS OF HYDROGEN CC PEROXIDE. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: HEME GROUP. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- MISCELLANEOUS: THIS IS ONE OF TWO CATALASES IN S.CEREVISIAE; THE CC OTHER IS CATALASE T, WHICH IS THE CYTOPLASMIC FORM. CC -!- SIMILARITY: BELONGS TO THE CATALASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13028; CAA31443.1; -. DR EMBL; Z68329; CAA92713.1; -. DR EMBL; Z70202; CAA94095.1; -. DR PIR; S07868; CSBYP. DR PDB; 1A4E; 13-AUG-99. DR SGD; S0002664; CTA1. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome; Multigene family; 3D-structure. FT ACT_SITE 70 70 FT ACT_SITE 143 143 FT BINDING 355 355 PROXIMAL HEME LIGAND. FT SITE 513 515 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 515 AA; 58555 MW; 22DFCC599D79801F CRC64; MSKLGQEKNE VNYSDVREDR VVTNSTGNPI NEPFVTQRIG EHGPLLLQDY NLIDSLAHFN RENIPQRNPH AHGSGAFGYF EVTDDITDIC GSAMFSKIGK RTKCLTRFST VGGDKGSADT VRDPRGFATK FYTEEGNLDW VYNNTPVFFI RDPSKFPHFI HTQKRNPQTN LRDADMFWDF LTTPENQVAI HQVMILFSDR GTPANYRSMH GYSGHTYKWS NKNGDWHYVQ VHIKTDQGIK NLTIEEATKI AGSNPDYCQQ DLFEAIQNGN YPSWTVYIQT MTERDAKKLP FSVFDLTKVW PQGQFPLRRV GKIVLNENPL NFFAQVEQAA FAPSTTVPYQ EASADPVLQA RLFSYADAHR YRLGPNFHQI PVNCPYASKF FNPAIRDGPM NVNGNFGSEP TYLANDKSYT YIQQDRPIQQ HQEVWNGPAI PYHWATSPGD VDFVQARNLY RVLGKQPGQQ KNLAYNIGIH VEGACPQIQQ RVYDMFARVD KGLSEAIKKV AEAKHASELS SNSKF // ID CISZ_YEAST STANDARD; PRT; 460 AA. AC P08679; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Citrate synthase, peroxisomal (EC 4.1.3.7). GN CIT2 OR YCR005C OR YCR5C OR YCR043. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92254505; PubMed=1580102; RA Biteau N., Fremaux C., Hebrard S., Menara A., Aigle M., Crouzet M.; RT "The complete sequence of a 10.8kb fragment to the right of the RT chromosome III centromere of Saccharomyces cerevisiae."; RL Yeast 8:61-70(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87089811; PubMed=3540614; RA Rosenkrantz M., Alam T., Kim K.-S., Clark B.J., Srere P.A., RA Guarente L.P.; RT "Mitochondrial and nonmitochondrial citrate synthases in RT Saccharomyces cerevisiae are encoded by distinct homologous genes."; RL Mol. Cell. Biol. 6:4509-4515(1986). RN [3] RP SEQUENCE OF 1-24 FROM N.A. RX MEDLINE=91094853; PubMed=1986232; RA Liao X., Small W.C., Srere P.A., Butow R.A.; RT "Intramitochondrial functions regulate nonmitochondrial citrate RT synthase (CIT2) expression in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 11:38-46(1991). CC -!- CATALYTIC ACTIVITY: CITRATE + COA = ACETYL-COA + H(2)O + CC OXALOACETATE. CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- MISCELLANEOUS: CITRATE SYNTHASE IS FOUND IN NEARLY ALL CELLS CC CAPABLE OF OXIDATIVE METABOLISM. CC -!- SIMILARITY: BELONGS TO THE CITRATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11113; CAA77442.1; -. DR EMBL; M14686; AAA34497.1; -. DR EMBL; M54982; AAA34498.1; -. DR EMBL; X59720; CAA42342.1; -. DR PIR; A25393; YKBYC. DR HSSP; P23007; 5CSC. DR YEPD; 5440; -. DR SGD; S0000598; CIT2. DR InterPro; IPR002020; Citrate_synt. DR Pfam; PF00285; citrate_synt; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. KW Lyase; Tricarboxylic acid cycle; Peroxisome; Multigene family. FT ACT_SITE 293 293 BY SIMILARITY. FT ACT_SITE 339 339 BY SIMILARITY. FT ACT_SITE 394 394 BY SIMILARITY. FT SITE 458 460 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 460 AA; 51413 MW; AB2F66AD9A9399EF CRC64; MTVPYLNSNR NVASYLQSNS SQEKTLKERF SEIYPIHAQD VRQFVKEHGK TKISDVLLEQ VYGGMRGIPG SVWEGSVLDP EDGIRFRGRT IADIQKDLPK AKGSSQPLPE ALFWLLLTGE VPTQAQVENL SADLMSRSEL PSHVVQLLDN LPKDLHPMAQ FSIAVTALES ESKFAKAYAQ GISKQDYWSY TFEDSLDLLG KLPVIAAKIY RNVFKDGKMG EVDPNADYAK NLVNLIGSKD EDFVDLMRLY LTIHSDHEGG NVSAHTSHLV GSALSSPYLS LASGLNGLAG PLHGRANQEV LEWLFALKEE VNDDYSKDTI EKYLWDTLNS GRVIPGYGHA VLRKTDPRYM AQRKFAMDHF PDYELFKLVS SIYEVAPGVL TEHGKTKNPW PNVDAHSGVL LQYYGLKESS FYTVLFGVSR AFGILAQLIT DRAIGASIER PKSYSTEKYK ELVKNIESKL // ID DAPT_HUMAN STANDARD; PRT; 680 AA. AC O15228; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Dihydroxyacetone phosphate acyltransferase (EC 2.3.1.42) (DHAP-AT) DE (DAP-AT) (Glycerone-phosphate O-acyltransferase) (Acyl- DE CoA:dihydroxyacetonephosphateacyltransferase). GN GNPAT OR DHAPAT OR DAPAT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=98119399; PubMed=9459311; RA Thai T.-P., Heid H., Rackwitz H.-R., Hunziker A., Gorgas K., RA Just W.W.; RT "Ether lipid biosynthesis: isolation and molecular characterization RT of human dihydroxyacetonephosphate acyltransferase."; RL FEBS Lett. 420:205-211(1997). RN [2] RP SEQUENCE FROM N.A., SEQUENCE OF 12-33, AND VARIANTS RCDP2 C-211;H-211. RX MEDLINE=98204809; PubMed=9536089; RA Ofman R., Hettema E.H., Hogenhout E.M., Caruso U., Muijsers A.O., RA Wanders R.J.A.; RT "Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the RT human cDNA and resolution of the molecular basis in rhizomelic RT chondrodysplasia punctata type 2."; RL Hum. Mol. Genet. 7:847-853(1998). CC -!- CATALYTIC ACTIVITY: ACYL-COA + GLYCERONE PHOSPHATE = COA + CC ACYLGLYCERONE PHOSPHATE. CC -!- PATHWAY: BIOSYNTHESIS OF ETHERLIPIDS (EPL) AND PLASMALOGENES. CC -!- SUBUNIT: MAY BE PART OF AN HETEROTRIMERIC COMPLEX COMPOSED OF DAP- CC AT, ADAP-S AND A MODIFIED FORM OF DAP-AT. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; EXCLUSIVELY LOCALIZED TO THE CC LUMENAL SIDE OF THE PEROXISOMAL MEMBRANE (BY SIMILARITY). CC -!- DISEASE: DEFECTS IN GNPAT ARE THE CAUSE OF RHIZOMELIC CC CHONDRODYSPLASIA PUNCTATA, TYPE 2 (RCDP2). THIS AUTOSOMAL CC RECESSIVE DISEASE IS CHARACTERIZED BY RHIZOMELIC SHORTENING OF THE CC UPPER EXTREMITIES, SEVERE GROWTH AND MENTAL RETARDATION AND CC CATARACT. CC -!- SIMILARITY: BELONGS TO THE GPAT / DAPAT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ002190; CAA05242.1; -. DR EMBL; AF043937; AAC24505.1; -. DR MIM; 602744; -. DR MIM; 222765; -. DR InterPro; IPR002123; Acyltransferase. DR Pfam; PF01553; Acyltransferase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Transferase; Acyltransferase; Peroxisome; Membrane; KW Rhizomelic chondrodysplasia punctata; Disease mutation. FT DOMAIN 3 9 POLY-SER. FT SITE 678 680 MICROBODY TARGETING SIGNAL (POTENTIAL). FT VARIANT 211 211 R -> C (IN RCDP2). FT /FTId=VAR_006357. FT VARIANT 211 211 R -> H (IN RCDP2). FT /FTId=VAR_006358. FT CONFLICT 26 26 S -> K (IN REF. 2; AA SEQUENCE). FT CONFLICT 31 31 K -> N (IN REF. 2; AA SEQUENCE). SQ SEQUENCE 680 AA; 77187 MW; BDF624CCD4D92477 CRC64; MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF AMKCYTPLVY KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR EEVSEILDEM SHKLRLGAIR FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF FLEGTRSRSA KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV PRYIPQKQSE DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM DFDALVEKTL WLKGLTQAFG GFLIWPDNKP AEEVVPASIL LHSNIASLVK DQVILKVDSG DSEVVDGLML QHITLLMCSA YRNQLLNIFV RPSLVAVALQ MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC YLLCKSEAIQ VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC IFNVNEPATT KLEEMLGCKT PIGKPATAKL // ID DAPT_MOUSE STANDARD; PRT; 678 AA. AC P98192; Q9WUT6; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Dihydroxyacetone phosphate acyltransferase (EC 2.3.1.42) (DHAP-AT) DE (DAP-AT) (Glycerone-phosphate O-acyltransferase) (Acyl- DE CoA:dihydroxyacetonephosphateacyltransferase). GN GNPAT OR DHAPAT. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; TISSUE=Fibroblast; RX MEDLINE=99326186; PubMed=10395968; RA Ofman R., Hogenhout E.M., Wanders R.J.A.; RT "Identification and characterization of the mouse cDNA encoding RT acyl-CoA:dihydroxyacetone phosphate acyltransferase."; RL Biochim. Biophys. Acta 1439:89-94(1999). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=99383224; PubMed=10456321; RA Thai T.P., Rodemer C., Worsch J., Hunziker A., Gorgas K., Just W.W.; RT "Synthesis of plasmalogens in eye lens epithelial cells."; RL FEBS Lett. 456:263-268(1999). CC -!- CATALYTIC ACTIVITY: ACYL-COA + GLYCERONE PHOSPHATE = COA + CC ACYLGLYCERONE PHOSPHATE. CC -!- PATHWAY: BIOSYNTHESIS OF ETHERLIPIDS AND PLASMALOGENES. CC -!- SUBUNIT: MAY BE PART OF AN HETEROTRIMERIC COMPLEX COMPOSED OF DAP- CC AT, ADAP-S AND A MODIFIED FORM OF DAP-AT. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; EXCLUSIVELY LOCALIZED TO THE CC LUMENAL SIDE OF THE PEROXISOMAL MEMBRANE (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN LIVER AND TESTIS. LOWER CC LEVELS IN HEART, BRAIN, LUNG AND KIDNEY. DETECTED IN SPLEEN. CC -!- SIMILARITY: BELONGS TO THE GPAT / DAPAT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF110769; AAD55351.1; -. DR EMBL; AJ132012; CAB41975.1; -. DR MGD; MGI:1343460; Gnpat. DR InterPro; IPR002123; Acyltransferase. DR Pfam; PF01553; Acyltransferase; 1. KW Transferase; Acyltransferase; Peroxisome; Membrane. FT DOMAIN 5 9 POLY-SER. FT SITE 676 678 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 678 AA; 76869 MW; FA7245A2DDD174FF CRC64; MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRHISDFKFA MKCYTPPLYR GITPCKPGDI KSIVLSSEEI NYVIKQLSRE SLTGVDVLRE EASEILEEMS HKLRIGAIRF FAFVLSKIFK QIFSKVCVNE EGIQKLQRAV QEHPVVLLPS HRSYIDFLML SFILYSYDLP VPVIAAGMDF LGMRVVSELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RCGYAPVEFF LEGTRSRAAK TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYEILGVP KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LNRNTYNLVP RCIPQKQPED VQAFVTEVAY KMQLLQIENL ALSPWLLVVT ILLQNQLSMD FDALVEKTLW LKGVTQVFGG FLLWPDNKLP EEVVQSSILL HSNLASLVKD QVVLKMNSGS SQVVNGLVPE HIALLMCSAY RNQLLNIFAR PSLVALALHM TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY LLCKAEAMQM AGKDIILTDK GTAVLQFLTS LFKPFVESYQ LLCRYLLHEE DYFGEKEYLV AARKFTRQLL DQGSSQCYDA LSSELQKNAL AAFVRLGVVE KKKVDSKYVY YVNGPATSKL EEMLGCKKPI GKPATAKL // ID DAPT_RAT STANDARD; PRT; 678 AA. AC Q9ES71; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Dihydroxyacetone phosphate acyltransferase (EC 2.3.1.42) (DHAP-AT) DE (DAP-AT) (Glycerone-phosphate O-acyltransferase) (Acyl- DE CoA:dihydroxyacetonephosphateacyltransferase). GN GNPAT OR DHAPAT. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RA Ofman R., Lajmir S., Wanders R.J.A.; RT "cDNA encoding rat dihydroxyacetonephosphate acyltransferase RT (DHAP-AT)."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ACYL-COA + GLYCERONE PHOSPHATE = COA + CC ACYLGLYCERONE PHOSPHATE. CC -!- PATHWAY: BIOSYNTHESIS OF ETHERLIPIDS AND PLASMALOGENES. CC -!- SUBUNIT: MAY BE PART OF AN HETEROTRIMERIC COMPLEX COMPOSED OF DAP- CC AT, ADAP-S AND A MODIFIED FORM OF DAP-AT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; EXCLUSIVELY LOCALIZED TO THE CC LUMENAL SIDE OF THE PEROXISOMAL MEMBRANE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GPAT / DAPAT FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF218826; AAG17548.1; -. DR InterPro; IPR002123; Acyltransferase. DR Pfam; PF01553; Acyltransferase; 1. KW Transferase; Acyltransferase; Peroxisome; Membrane. FT DOMAIN 5 9 POLY-SER. FT SITE 676 678 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 678 AA; 77075 MW; F825A2728D534B68 CRC64; MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRQVSDFKFA MKCYTPPLYR GITPCKPSDI KSIVLNSEEI NYVIKQLSRE SLTGVDVLRE EANEILEEMS HKLRIGAIRF FAFVLSKVFK QIFSKVCVNE EGIQKLQRAI QEHPVILLPS HRSYIDFLML SFVLYNYDLP VPVIAAGMDF LGMRVVSELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RSGYAPVEFF LEGTRSRAAK TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYELLGIP KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LSRNTYNLVP RCIPQKQPED VQAFVTEVAY KMQLLQIENL ALSPWLLVVA ILLQNQLCMD FDALVEKTLW LKGLTQVFGG FLLWPDNKLP EEVVQSSILL HSNLATLVKD QVVLKVDSES SQMVNGLVPQ HIAFLMCSAY RNQLLNVFAR PSLVAVALHM TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY LLCKTEVMQM TGKDIILTDK GNAVLQFLTG LFKPFVESYQ ILSKCLLHEE DYFSEKEYLV TARKFTRQLL DQDASQCYDA LSSELQKNAL AAFVRLGVVE KNKVDSKYVY YVNGPATSKL EEMLGCKKPI GKPATAKL // ID DAS_PICAN STANDARD; PRT; 710 AA. AC P06834; DT 01-JAN-1988 (Rel. 06, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Dihydroxy-acetone synthase (EC 2.2.1.3) (DHAS) (Formaldehyde DE transketolase) (Glycerone synthase). GN DAS. OS Pichia angusta (Yeast) (Hansenula polymorpha). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4905; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 34438; RX MEDLINE=85215670; PubMed=2987872; RA Janowicz Z.A., Eckart M.R., Drewke C., Roggenkamp R.O., RA Hollenberg C.P., Maat J., Ledeboer A.M., Visser C., Verrips C.T.; RT "Cloning and characterization of the DAS gene encoding the major RT methanol assimilatory enzyme from the methylotrophic yeast Hansenula RT polymorpha."; RL Nucleic Acids Res. 13:3043-3062(1985). RN [2] RP REVISIONS, SEQUENCE OF 667-710 FROM N.A. RC STRAIN=ATCC 34438; RX MEDLINE=93101130; PubMed=1465101; RA Hansen H., Didion T., Thiemann A., Veenhuis M., Roggenkamp R.O.; RT "Targeting sequences of the two major peroxisomal proteins in the RT methylotrophic yeast Hansenula polymorpha."; RL Mol. Gen. Genet. 235:269-278(1992). CC -!- FUNCTION: THIS IS THE MAJOR METHANOL ASSIMILATORY ENZYME FROM CC THE METHYLOTROPHIC HANSENULA POLYMORPHA. CC -!- CATALYTIC ACTIVITY: D-XYLULOSE 5-PHOSPHATE + FORMALDEHYDE = CC GLYCERALDEHYDE 3-PHOSPHATE + GLYCERONE. CC -!- COFACTOR: THIAMINE PYROPHOSPHATE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE TRANSKETOLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02424; CAA26276.1; -. DR PIR; A23009; XJHQFK. DR HSSP; P23254; 1AY0. DR InterPro; IPR000360; Transketolase. DR Pfam; PF00456; transketolase; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Methanol utilization; Peroxisome; Transferase; Thiamine pyrophosphate. FT SITE 708 710 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 710 AA; 78842 MW; E4424B6D37CC8B0B CRC64; MSMRIPKAAS VNDEQHQRII KYGRALVLDI VEQYGGGHPG SAMGAMAIGI ALWKYTLKYA PNDPNYFNRD RFVLSNGHVC LFQYIFQHLY GLKSMTMAQL KSYHSNDFHS LCPGHPEIEH DAVEVTTGPL GQGISNSVGL AIATKNLAAT YNKPGFDIIT NKVYCMVGDA CLQEGPALES ISLAGHMGLD NLIVLYDNNQ VCCDGSVDIA NTEDISAKFK ACNWNVIEVE NASEDVATIV KALEYAQAEK HRPTLINCRT VIGSGAAFEN HCAAHGNALG EDGVRELKIK YGMNPAQKFY IPQDVYDFFK EKPAEGDKLV AEWKSLVAKY VKAYPEEGQE FLARMRGELP KNWKSFLPQQ EFTGDAPTRA AARELVRALG QNCKSVIAGC ADLSVSVNLQ WPGVKYFMDP SLSTQCGLSG DYSGRYIEYG IREHAMCAIA NGLAAYNKGT FLPITSTFFM FYLYAAPAIR MAGLQELKAI HIGTHDSINE GENGPTHQPV ESPALFRAYA NIYYMRPVDS AEVFGLFQKA VELPFSSILS LSRNEVLQYL ASRAQRRRNA AGYILEDAEN AEVQIIGVGA EMEFADKAAK ILGRKFRTRV LSIPCTRLFD EQSIGYRRSV LRKDGRQVPT VVVDGHVAFG WERYATASYC MNTYGKSLPP EVIYEYFGYN PATIAKKVEA YVRACQRDPL LLHDFLDLKE KPNHDKVNKL // ID DCMC_HUMAN STANDARD; PRT; 493 AA. AC O95822; Q9Y3F2; Q9UNU5; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Malonyl-CoA decarboxylase, mitochondrial precursor (EC 4.1.1.9) (MCD). GN MLYCD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE OF 40-493 FROM N.A. RX MEDLINE=99347936; PubMed=10417274; RA FitzPatrick D.R., Hill A., Tolmie J.L., Thorburn D.R., RA Christodoulou J.; RT "The molecular basis fo malonyl-CoA decarboxylase deficiency."; RL Am. J. Hum. Genet. 65:318-326(1999). RN [2] RP SEQUENCE OF 40-493 FROM N.A. RX MEDLINE=99386915; PubMed=10455107; RA Sacksteder K.A., Morrell J.C., Wanders R.J.A., Matalon R., Gould S.J.; RT "MCD encodes peroxisomal and cytoplasmic forms of malonyl-CoA RT decarboxylase and is mutated in malonyl-CoA decarboxylase RT deficiency."; RL J. Biol. Chem. 274:24461-24468(1999). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=99088071; PubMed=9869665; RA Gao J., Waber L., Bennett M.J., Gibson K.M., Cohen J.C.; RT "Cloning and mutational analysis of human malonyl-coenzyme A RT decarboxylase."; RL J. Lipid Res. 40:178-182(1999). CC -!- FUNCTION: CATALYZES THE CONVERSION OF MALONYL-COA TO ACETYL-COA. CC IN THE FATTY ACID BIOSYNTHESIS MCD SELECTIVELY REMOVES MALONYL-COA CC AND THUS ASSURES THAT METHYL-MALONYL-COA IS THE ONLY CHAIN CC ELONGATING SUBSTRATE FOR FATTY ACID SYNTHASE AND THAT FATTY ACIDS CC WITH MULTIPLE METHYL SIDE CHAINS ARE PRODUCED. IN PEROXISOMES IT CC MAY BE INVOLVED IN DEGRADING INTRAPEROXISOMAL MALONYL-COA, WHICH CC IS GENERATED BY THE PEROXISOMAL BETA-OXIDATION OF ODD CHAIN-LENGTH CC DICARBOXYLIC FATTY ACIDS. CC -!- CATALYTIC ACTIVITY: MALONYL-COA = ACETYL-COA + CO(2). CC -!- PATHWAY: FATTY ACID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL, CYTOPLASMIC AND PEROXISOMAL. CC -!- ALTERNATIVE PRODUCTS: A SINGLE NUCLEAR GENE PRODUCES BOTH FORMS CC BY USE OF ALTERNATIVE INITIATION CODONS IN THE SAME READING FRAME. CC -!- DISEASE: DEFECTS IN MLYCD ARE THE CAUSE OF MALONYL-COA CC DECARBOXYLASE DEFICIENCY; AN AUTOSOMAL RECESSIVE DISEASE CC CHARACTERIZED BY ABDOMINAL PAIN, CHRONIC CONSTIPATION, EPISODIC CC VOMITING, METABOLIC ACIDOSIS AND MALONIC ACIDURIA. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF097832; AAD16177.2; -. DR EMBL; AF153679; AAD34631.1; -. DR EMBL; AF090834; AAD48994.1; -. DR MIM; 248360; -. KW Lyase; Decarboxylase; Fatty acid biosynthesis; Mitochondrion; KW Transit peptide; Peroxisome; Alternative initiation. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 493 MALONYL-COA DECARBOXYLASE, MITOCHONDRIAL. FT CHAIN 40 493 MALONYL-COA DECARBOXYLASE, FT CYTOPLASMIC/PEROXISOMAL. FT INIT_MET 40 40 FOR CYTOPLASMIC/PEROXISOMAL ISOFORM. FT SITE 491 493 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 82 82 A -> D (IN REF. 1). FT CONFLICT 119 119 A -> S (IN REF. 3). FT CONFLICT 127 127 D -> V (IN REF. 3). FT CONFLICT 192 192 S -> P (IN REF. 2). FT CONFLICT 297 307 GLQGVELGTFL -> DSKGWSWEHSS (IN REF. 1). SQ SEQUENCE 493 AA; 55003 MW; 8F061CA38908E8FC CRC64; MRGFGPGLTA RRLLPLRLPP RPPGPRLASG QAAGALERAM DELLRRAVPP TPAYELREKT PAPAEGQCAD FVSFYGGLAE TAQRAELLGR LARGFGVDHG QVAEQSAGVL HLRQQQREAA VLLQAEDRLR YALVPRYRGL FHHISKLDGG VRFLVQLRAD LLEAQALKLV EGPDVREMNG VLKGMLSEWF SSGFLNLERV TWHSPCEVLQ KISEAEAVHP VKNWMDMKRR VGPYRRCYFF SHCSTPGEPL VVLHVALTGD ISSNIQAIVK EHPPSETEEK NKITAAIFYS ISLTQQGLQG VELGTFLIKR VVKELQREFP HLGVFSSLSP IPGFTKWLLG LLNSQTKEHG RNELFTDSEC KEISEITGGP INETLKLLLS SSEWVQSEKL VRALQTPLMR LCAWYLYGEK HRGYALNPVA NFHLQNGAVL WRINWMADVS LRGITGSCGL MANYRYFLEE TGPNSTSYLG SKIIKASEQV LSLVAQFQKN SKL // ID DHAB_HORVU STANDARD; PRT; 505 AA. AC Q40024; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Betaine-aldehyde dehydrogenase (EC 1.2.1.8) (BADH). OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95195158; PubMed=7888620; RA Ishitani M., Nakamura T., Han S.Y., Takabe T.; RT "Expression of the betaine aldehyde dehydrogenase gene in barley in RT response to osmotic stress and abscisic acid."; RL Plant Mol. Biol. 27:307-315(1995). CC -!- CATALYTIC ACTIVITY: BETAINE ALDEHYDE + NAD(+) + H(2)O = BETAINE CC + NADH. CC -!- PATHWAY: LAST STEP IN THE BIOSYNTHESIS OF BETAINE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE ALDEHYDE DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D26448; BAA05466.1; -. DR HSSP; P20000; 1A4Z. DR InterPro; IPR002086; Aldehyde_dehydr. DR Pfam; PF00171; aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. KW Oxidoreductase; NAD; Peroxisome. FT NP_BIND 239 244 NAD (ADP PART) (BY SIMILARITY). FT ACT_SITE 261 261 BY SIMILARITY. FT ACT_SITE 296 296 BY SIMILARITY. FT SITE 503 505 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 505 AA; 54289 MW; C30B40FF22413BB6 CRC64; MAAPPAIPRR GLFIGGGWRE PTLGRHIPVI NPATEDTIGD IPAATAEDVE LAVAAGGPVL ARRREPWARA SGATRAKYLN AIAAKITGKI AYLALLETVD SGKPKDEAVA DMDDVAACFE YYAALAEALD GKQHAPISLP MEEFKTYVLK EPIGVVGLIT PWNYPLLMAT WKVAPALAAG CTAVLKPSEL ASLTCLELGA ICEEIGLPSG VLNIITGLGP DAGAPIASHP HVDKIAFTGS TATGKTIMTA AAQMVKPVSL ELGGKSPLVT FDDVADIDKA VEWPMLGCFF NGGQVCSATS RLLLHEKIAE PFLDRLVEWA KNIKISDPLE EGCRLGSVIS KGQYEQIKKF ISTARSEGAT ILHGGDRPKH LGKGFFIEPT INTGVSTSMQ IWREEVFGPV ICVKVFKTES EAVELANDTH YGLAGGVISD DLERCERIAK VIHSGIVWKN CSQPTLVQAP WGGNKRSGFG RELGEWGLEN YLSVKQVTRY CKDELYGWYQ RPSKL // ID DHAB_ORYSA STANDARD; PRT; 505 AA. AC O24174; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Betaine-aldehyde dehydrogenase (EC 1.2.1.8) (BADH). OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. NIPPONBARE; RX MEDLINE=97336302; PubMed=9193078; RA Nakamura T., Yokota S., Muramoto Y., Tsutsui K., Oguri Y., Fukui K., RA Takabe T.; RT "Expression of a betaine aldehyde dehydrogenase gene in rice, a RT glycinebetaine nonaccumulator, and possible localization of its RT protein in peroxisomes."; RL Plant J. 11:1115-1120(1997). CC -!- CATALYTIC ACTIVITY: BETAINE ALDEHYDE + NAD(+) + H(2)O = BETAINE CC + NADH. CC -!- PATHWAY: LAST STEP IN THE BIOSYNTHESIS OF BETAINE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE ALDEHYDE DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB001348; BAA21098.1; -. DR InterPro; IPR002086; Aldehyde_dehydr. DR Pfam; PF00171; aldedh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. KW Oxidoreductase; NAD; Peroxisome. FT NP_BIND 240 245 NAD (ADP PART) (BY SIMILARITY). FT ACT_SITE 262 262 BY SIMILARITY. FT ACT_SITE 296 296 BY SIMILARITY. FT SITE 503 505 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 505 AA; 54647 MW; 85EFA42B059A8081 CRC64; MAAPSAIPRR GLFIGGGWRE PSLGRRLPVV NPATEATIGD IPAATAEDVE LAVSAARDAF GRDGGRHWSR APGAVRAKYL KAIAAKIKDK KSYLALLETL DSGKPLDEAA GDMEDVAACF EYYADLAEAL DGKQRAPISL PMENFESYVL KEPIGVVGLI TPWNYPLLMA TWKVAPALAA GCTAVLKPSE LASLTCLELG GICAEIGLPP GVLNIITGLG TEAGAPLASH PHVDKIAFTG STETGKRIMI TASQMVKPVS LELGGKSPLI VFDDVDIDKA VEWAMFGCFA NAGQVCSATS RLLLHEKIAK RFLDRLVAWA KSIKISDPLE EGCRLGSVVS EGQYQKIMKF ISTARCEGAT ILYGGARPQH LKRGFFIEPT IITNVSTSMQ IWREEVFGPV ICVKEFRTER EAVELANDTH YGLAGAVISN DLERCERISK AIQSGIVWIN CSQPCFVQAP WGGNKRSGFG RELGQWGLDN YLSVKQVTKY CSDEPYGWYR PPSKL // ID ECH1_HUMAN STANDARD; PRT; 328 AA. AC Q13011; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Delta3,5-delta2,4-dienoyl-CoA isomerase, mitochondrial precursor DE (EC 5.3.3.-). GN ECH1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Retina; RX MEDLINE=96047331; PubMed=7558027; RA Fitzpatrick D.R., Germain-Lee E., Valle D.; RT "Isolation and characterization of rat and human cDNAs encoding a RT novel putative peroxisomal enoyl-CoA hydratase."; RL Genomics 27:457-466(1995). RN [2] RP SEQUENCE FROM N.A. RA Fitzpatrick D.R., Valle D.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ISOMERIZATION OF 3-TRANS,5-CIS-DIENOYL-COA TO 2-TRANS,4- CC TRANS-DIENOYL-COA (BY SIMILARITY). CC -!- PATHWAY: AUXILIARY STEP IN THE FATTY ACID BETA-OXIDATION PATHWAY. CC -!- SUBUNIT: HOMOHEXAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL AND PEROXISOMAL (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ENOYL-COA HYDRATASE/ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U16660; AAC50222.1; -. DR EMBL; AF030249; AAB86485.1; -. DR EMBL; AF030246; AAB86485.1; JOINED. DR EMBL; AF030247; AAB86485.1; JOINED. DR EMBL; AF030248; AAB86485.1; JOINED. DR HSSP; P14604; 2DUB. DR MIM; 600696; -. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Isomerase; Peroxisome; Mitochondrion; KW Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (BY SIMILARITY). FT CHAIN ? 328 DELTA3,5-DELTA2,4-DIENOYL-COA ISOMERASE. FT ACT_SITE 177 177 ACTIVATES A WATER MOLECULE (BY FT SIMILARITY). FT ACT_SITE 197 197 PROTON ACCEPTOR (BY SIMILARITY). FT ACT_SITE 205 205 PROTON DONOR (BY SIMILARITY). FT SITE 326 328 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 328 AA; 35994 MW; 29A22AF26DFFA566 CRC64; MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA PDHSYESLRV TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA DCRAVVISGA GKMFTAGIDL MDMASDILQP KGDDVARISW YLRDIITRYQ ETFNVIERCP KPVIAAVHGG CIGGGVDLVT ACDIRYCAQD AFFQVKEVDV GLAADVGTLE RLPKVIGNQS LVNELAFTAH KMMADEALDS GLVSRVFPDK EVMLDAALPL APEISSKTTV LVQSTKVNLL YSRDHSVAES LNYVASWNMS MLQTQDLVKS VQPTTENKEL KTVTFSKL // ID ECH1_MOUSE STANDARD; PRT; 327 AA. AC O35459; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Delta3,5-delta2,4-dienoyl-CoA isomerase, mitochondrial precursor DE (EC 5.3.3.-). GN ECH1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RA Fitzpatrick D.R.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ISOMERIZATION OF 3-TRANS,5-CIS-DIENOYL-COA TO 2-TRANS,4- CC TRANS-DIENOYL-COA (BY SIMILARITY). CC -!- PATHWAY: AUXILIARY STEP IN THE FATTY ACID BETA-OXIDATION PATHWAY. CC -!- SUBUNIT: HOMOHEXAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL AND PEROXISOMAL (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ENOYL-COA HYDRATASE/ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF030343; AAB84224.1; -. DR MGD; MGI:1858208; Ech1. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Isomerase; Peroxisome; Mitochondrion; KW Transit peptide. FT TRANSIT 1 ? MITOCHONDRION (BY SIMILARITY). FT CHAIN ? 327 DELTA3,5-DELTA2,4-DIENOYL-COA ISOMERASE. FT ACT_SITE 176 176 ACTIVATES A WATER MOLECULE (BY FT SIMILARITY). FT ACT_SITE 196 196 PROTON ACCEPTOR (BY SIMILARITY). FT ACT_SITE 204 204 PROTON DONOR (BY SIMILARITY). FT SITE 325 327 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 327 AA; 36118 MW; CC0E612C74FBEE2E CRC64; MATAMTVSSK LRGLLMQQLR GTSQLYFNIS LRSLSSSAQE ASKRAPEEVS DHNYESIQVT SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM DMASELMQPS GDDAARIAWY LRDLISKYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLVSA CDIRYCTQDA FFQIKEVDMG LAADVGTLQR LPKVIGNQSL VNELTFSARK MMADEALDSG LVSRVFQDKD AMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM LQTQDIIKSV QAAMEKRDTK SITFSKL // ID ECH1_RAT STANDARD; PRT; 327 AA. AC Q62651; DT 01-NOV-1997 (Rel. 35, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Delta3,5-delta2,4-dienoyl-CoA isomerase, mitochondrial precursor DE (EC 5.3.3.-). GN ECH1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Liver; RX MEDLINE=96047331; PubMed=7558027; RA Fitzpatrick D.R., Germain-Lee E., Valle D.; RT "Isolation and characterization of rat and human cDNAs encoding a RT novel putative peroxisomal enoyl-CoA hydratase."; RL Genomics 27:457-466(1995). RN [2] RP CHARACTERIZATION. RC TISSUE=Liver; RX MEDLINE=98079067; PubMed=9417087; RA Filppula S.A., Yagi A.I., Kilpeleainen S.H., Novikov D., RA Fitzpatrick D.R., Vihinen M., Valle D., Hiltunen J.K.; RT "Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular RT characterization."; RL J. Biol. Chem. 273:349-355(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND REVISION TO 164. RC STRAIN=WISTAR; TISSUE=Liver; RX MEDLINE=98416692; PubMed=9739087; RA Modis Y., Filppula S.A., Novikov D.K., Norledge B., Hiltunen J.K., RA Wierenga R.K.; RT "The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution RT reveals the importance of aspartate and glutamate sidechains for RT catalysis."; RL Structure 6:957-970(1998). CC -!- FUNCTION: ISOMERIZATION OF 3-TRANS,5-CIS-DIENOYL-COA TO 2-TRANS,4- CC TRANS-DIENOYL-COA. CC -!- PATHWAY: AUXILIARY STEP IN THE FATTY ACID BETA-OXIDATION PATHWAY. CC -!- SUBUNIT: HOMOHEXAMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL AND PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE ENOYL-COA HYDRATASE/ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08976; AAA82008.1; -. DR PDB; 1DCI; 30-MAR-99. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Isomerase; Peroxisome; Mitochondrion; KW Transit peptide; 3D-structure; Zinc-finger. FT TRANSIT 1 ? MITOCHONDRION (BY SIMILARITY). FT CHAIN ? 327 DELTA3,5-DELTA2,4-DIENOYL-COA ISOMERASE. FT ACT_SITE 176 176 ACTIVATES A WATER MOLECULE. FT ACT_SITE 196 196 PROTON ACCEPTOR. FT ACT_SITE 204 204 PROTON DONOR. FT SITE 325 327 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 164 164 A -> T (IN REF. 1). SQ SEQUENCE 327 AA; 36171 MW; 6FAE35D7D5F66BC2 CRC64; MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS DHNYESIQVT SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM DMASDILQPP GDDVARIAWY LRDLISRYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLISA CDIRYCTQDA FFQVKEVDVG LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG LVSRVFPDKD VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM LQTQDIIKSV QAAMEKKDSK SITFSKL // ID ECHP_CAVPO STANDARD; PRT; 725 AA. AC P55100; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Peroxisomal bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA DE hydratase (EC 4.2.1.17); 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8); DE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]. GN EHHADH. OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Hystricognathi; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=96140708; PubMed=8549802; RA Caira F., Cherkaoui-Malki M., Hoefler G., Latruffe N.; RT "Cloning and tissue expression of two cDNAs encoding the peroxisomal RT 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea RT pig liver."; RL FEBS Lett. 378:57-60(1996). CC -!- CATALYTIC ACTIVITY: (3S)-3-HYDROXYACYL-COA = TRANS-2(OR 3)-ENOYL- CC COA + H(2)O. CC -!- CATALYTIC ACTIVITY: L-3-HYDROXYACYL-COA + NAD(+) = 3-OXOACYL-COA + CC NADH. CC -!- CATALYTIC ACTIVITY: 3-ENOYL-COA = 2-TRANS-ENOYL-COA. CC -!- PATHWAY: CATALYZES THREE STEPS OF THE FATTY ACID BETA-OXIDATION CC CYCLE. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE ENOYL-COA CC HYDRATASE/ISOMERASE FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE 3- CC HYDROXYACYL-COA DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X92742; CAA63403.1; -. DR EMBL; X85112; CAA59431.1; -. DR HSSP; P14604; 2DUB. DR InterPro; IPR002135; 3HCDH. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Multifunctional enzyme; Oxidoreductase; NAD; KW Lyase; Isomerase; Peroxisome. FT INIT_MET 0 0 BY SIMILARITY. FT DOMAIN 1 283 ENOYL-COA HYDRATASE / ISOMERASE. FT DOMAIN 284 574 3-HYDROXYACYL-COA DEHYDROGENASE. FT ACT_SITE 105 105 ACTIVATES A WATER MOLECULE (BY FT SIMILARITY). FT ACT_SITE 125 125 PROVIDES THE ALPHA-PROTON (BY FT SIMILARITY). FT SITE 723 725 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 725 AA; 79243 MW; 645FC94CAF314E17 CRC64; AEYLRLPHSL ALIRLRNPPV NAISPAVIHG IKEGLQKAMS DYTIKGIVIS GANNIFCAGA DIHGFSAPLS FGTGSGLGPI VDEMQRYEKP VVAAIQGMAL GGGLELSLGC HYRIAHAEAR IGFPEVTLGI LPGARGTQLL PRLIGVPAAL DLITSGRHIT AGEALKLGIL DKVVNSAPVE EAIKFAQKIL NQPLEPRRIL NRPVSSLPNM DAIFGEAVEK MRRQHPGQLA PETCVRSVQA SVQYPYEGGI MKERELFLNL QHSGQAKALQ YAFFAERSAP KWSTPSGASW KTAAARPVSS VGVLGLGTMG RGIAISFARV GIPVIAVESD PKQLETAQKL ITSILEKEAS KSRQQCGQQR SGPKPRFSSS MKDLASVDLV VEAVFEDMNL KKRVFAELSA VCKPEAFLCT NTSALDVDEI ATSTNRPQQV IGTHFFSPAH VMKLLEVIPS RHSSPTTIAT VMDLAKKIKK VAVVVGNCYG FVGNRMLRSY YEQTNFLLED GSKPEDIDQA LEEFGFRMGP FRVSDLAGLD VGWKIRKGQG LTGPSLQGTA PARKRGNARY SPIADMLCEL GRFGQKTGQG WYKYDKPLGR IHKPDPWLSK FLSEYRETHH IKPRVIGRDE ILERCLYALI NEAFRILGEG IAASPEHIDV IYLHGYGWPR HKGGPMFYAA SVGLPTVLEK LQKYYQQNPD IPHLEPCNYL KKLASQGNPP LKEWQSLAGL PSSKL // ID ECHP_HUMAN STANDARD; PRT; 722 AA. AC Q08426; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA DE hydratase (EC 4.2.1.17); 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8); DE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]. GN EHHADH OR ECHD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=94245181; PubMed=8188243; RA Hoefler G., Forstner M., McGuinness M.C., Hulla W., Hiden M., RA Krisper P., Kenner L., Ried T., Lengauer C., Zechner R., Moser H.W., RA Chen G.L.; RT "cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3- RT hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to RT chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' RT noncoding region."; RL Genomics 19:60-67(1994). RN [2] RP SEQUENCE OF 501-722 FROM N.A. RC TISSUE=Liver; RX MEDLINE=91337043; PubMed=1651711; RA Chen G.L., Balfe A., Erwa W., Hoefler G., Gaertner J., Aikawa J., RA Chen W.W.; RT "Import of human bifunctional enzyme into peroxisomes of human RT hepatoma cells in vitro."; RL Biochem. Biophys. Res. Commun. 178:1084-1091(1991). CC -!- CATALYTIC ACTIVITY: (3S)-3-HYDROXYACYL-COA = TRANS-2(OR 3)-ENOYL- CC COA + H(2)O. CC -!- CATALYTIC ACTIVITY: L-3-HYDROXYACYL-COA + NAD(+) = 3-OXOACYL-COA + CC NADH. CC -!- CATALYTIC ACTIVITY: 3-ENOYL-COA = 2-TRANS-ENOYL-COA. CC -!- PATHWAY: CATALYZES THREE STEPS OF THE FATTY ACID BETA-OXIDATION CC CYCLE. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: LIVER AND KIDNEY. LOWER AMOUNTS SEEN IN THE CC BRAIN. CC -!- DISEASE: ABSENT IN PATIENTS SUFFERING WITH PEROXISOMAL DISORDERS CC SUCH AS ZELLWEGER SYNDROME, NEONATAL ADRENOLEUKODYSTROPHY AND CC INFANTILE REFSUMS DISEASE. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE ENOYL-COA CC HYDRATASE/ISOMERASE FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE 3- CC HYDROXYACYL-COA DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07077; AAA53289.1; -. DR EMBL; S50245; AAB19482.1; -. DR HSSP; P14604; 2DUB. DR MIM; 261515; -. DR InterPro; IPR002135; 3HCDH. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Multifunctional enzyme; Oxidoreductase; NAD; KW Lyase; Isomerase; Peroxisome; Zellweger syndrome. FT INIT_MET 0 0 BY SIMILARITY. FT DOMAIN 1 281 ENOYL-COA HYDRATASE / ISOMERASE. FT DOMAIN 282 571 3-HYDROXYACYL-COA DEHYDROGENASE. FT ACT_SITE 103 103 ACTIVATES A WATER MOLECULE (BY FT SIMILARITY). FT ACT_SITE 123 123 PROVIDES THE ALPHA-PROTON (BY FT SIMILARITY). FT SITE 720 722 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 722 AA; 79208 MW; 013F00B887BFCCDD CRC64; AEYTRLHNAL ALIRLRNPPV NAISTTLLRD IKEGLQKAGR DHTIKAIVIC GAEGKFSAGA DIRGFSAPRT FGLILGHVVD EIQRNEKPVV AAIQGMAFGG GLELALGCHY RIAHADAQVG LPEVTLGLLP GARGTQLLPR LTGVPAALDL ITSGRRILAD EALKLGILDK VVNSDPVEEA IRFAQRVSDQ PLESRRLCNK PIQSLPNMDS IFSEALLKMR RQHPGCLAQE ACVRAVQAAV QYPYEVGIKK EEELFLYLLQ SGQARALQYA FFAERKANKW STPSGASWKT ASARPVSSVG VVGLGTMGRG IVISFARARI PVIGVDSDKN QLATANKMIT SVLEKEASKM QQSGHPWSGP KPRLTSSVKE LGGVDLVIEA VFEEMSLKKQ VFAELSAVCK PEAFLCTNTS ALDVDEIASS TDRPHLVIGT HFFSPAHVMK LLEVIPSQYS SPTTIATVMN LSKKIKKIGV VVGNCFGFVG NRMLNPYYNQ AYFLLEEGSK PEEVDQVLEE FGFKMGPFRV SDLAGLDVGW KSRKGQGLTG PTLLPGTPAR KRGNRRYCPI PDVLCELGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS RYRKPHHIEP RTISQDEILE RCLYSLINEA FRILGEGIAA SPEHIDVVYL HGYGCARHKG GPMFYASTVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLKKL ASQGNPPLKE WQSLAGSPSS KL // ID ECHP_RAT STANDARD; PRT; 721 AA. AC P07896; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Peroxisomal bifunctional enzyme (PBE) (PBFE) [Includes: Enoyl-CoA DE hydratase (EC 4.2.1.17); 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8); DE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]. GN EHHADH. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85261258; PubMed=4019459; RA Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S., RA Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T.; RT "Molecular cloning and nucleotide sequence of the cDNA for rat RT peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase RT bifunctional enzyme."; RL J. Biol. Chem. 260:8905-8910(1985). RN [2] RP SEQUENCE OF 1-23 FROM N.A. RX MEDLINE=87250406; PubMed=3036802; RA Ishii N., Hijikata M., Osumi T., Hashimoto T.; RT "Structural organization of the gene for rat enoyl-CoA hydratase:3- RT hydroxyacyl-CoA dehydrogenase bifunctional enzyme."; RL J. Biol. Chem. 262:8144-8150(1987). RN [3] RP ISOMERASE ACTIVITY. RX MEDLINE=90153855; PubMed=2303409; RA Palosaari P.M., Hiltunen J.K.; RT "Peroxisomal bifunctional protein from rat liver is a trifunctional RT enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA RT dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities."; RL J. Biol. Chem. 265:2446-2449(1990). CC -!- CATALYTIC ACTIVITY: (3S)-3-HYDROXYACYL-COA = TRANS-2(OR 3)-ENOYL- CC COA + H(2)O. CC -!- CATALYTIC ACTIVITY: L-3-HYDROXYACYL-COA + NAD(+) = 3-OXOACYL-COA + CC NADH. CC -!- CATALYTIC ACTIVITY: 3-ENOYL-COA = 2-TRANS-ENOYL-COA. CC -!- PATHWAY: CATALYZES THREE STEPS OF THE FATTY ACID BETA-OXIDATION CC CYCLE. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE ENOYL-COA CC HYDRATASE/ISOMERASE FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE 3- CC HYDROXYACYL-COA DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K03249; AAA41825.1; -. DR EMBL; J02748; AAA41826.1; -. DR PIR; A23575; DWRTEP. DR HSSP; P14604; 2DUB. DR InterPro; IPR002135; 3HCDH. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Multifunctional enzyme; Oxidoreductase; NAD; KW Lyase; Isomerase; Peroxisome. FT INIT_MET 0 0 FT MOD_RES 1 1 BLOCKED. FT DOMAIN 1 280 ENOYL-COA HYDRATASE / ISOMERASE. FT DOMAIN 281 570 3-HYDROXYACYL-COA DEHYDROGENASE. FT ACT_SITE 102 102 ACTIVATES A WATER MOLECULE (BY FT SIMILARITY). FT ACT_SITE 122 122 PROVIDES THE ALPHA-PROTON (BY FT SIMILARITY). FT SITE 719 721 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 721 AA; 78526 MW; 0FB1D6ED3CE58626 CRC64; AEYLRLPHSL AMIRLCNPPV NAVSPTVIRE VRNGLQKAGS DHTVKAIVIC GANGNFCAGA DIHGFSAFTP GLALGSLVDE IQRYQKPVLA AIQGVALGGG LELALGCHYR IANAKARVGL PEVTLGILPG ARGTQLLPRV VGVPVALDLI TSGKYLSADE ALRLGILDAV VKSDPVEEAI KFAQKIIDKP IEPRRIFNKP VPSLPNMDSV FAEAIAKVRK QYPGVLAPET CVRSIQASVK HPYEVGIKEE EKLFMYLRAS GQAKALQYAF FAEKSANKWS TPSGASWKTA SAQPVSSVGV LGLGTMGRGI AISFARVGIS VVAVESDPKQ LDAAKKIITF TLEKEASRAH QNGQASAKPK LRFSSSTKEL STVDLVVEAV FEDMNLKKKV FAELSALCKP GAFLCTNTSA LNVDDIASST DRPQLVIGTH FFSPAHVMRL LEVIPSRYSS PTTIATVMSL SKKIGKIGVV VGNCYGFVGN RMLAPYYNQG FFLLEEGSKP EDVDGVLEEF GFKMGPFRVS DLAGLDVGWK IRKGQGLTGP SLPPGTPVRK RGNSRYSPLG DMLCEAGRFG QKTGKGWYQY DKPLGRIHKP DPWLSTFLSQ YREVHHIEQR TISKEEILER CLYSLINEAF RILEEGMAAR PEHIDVIYLH GYGWPRHKGG PMFYAASVGL PTVLEKLQKY YRQNPDIPQL EPSDYLRRLV AQGSPPLKEW QSLAGPHGSK L // ID FAT2_YEAST STANDARD; PRT; 543 AA. AC P38137; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal-coenzyme A synthetase (EC 6.-.-.-). GN FAT2 OR PCS60 OR YBR222C OR YBR1512. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RA Dubois E., el Bakkoury M., Glansdorff N., Messenguy F., Pierard A., RA Scherens B., Vierendeels F.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP PARTIAL SEQUENCE, AND CHARACTERIZATION. RC STRAIN=S288C; RX MEDLINE=96439079; PubMed=8841414; RA Blobel F., Erdmann R.; RT "Identification of a yeast peroxisomal member of the family of AMP- RT binding proteins."; RL Eur. J. Biochem. 240:468-476(1996). CC -!- FUNCTION: NON-ESSENTIAL PROTEIN INVOLVED IN FATTY ACID METABOLISM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL MATRIX AND AT THE PEROXISOMAL CC PERIPHERAL MEMBRANE. CC -!- INDUCTION: BY OLEIC ACID. CC -!- SIMILARITY: BELONGS TO THE ATP-DEPENDENT AMP-BINDING ENZYME CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z36091; CAA85185.1; -. DR PIR; S46098; S46098. DR HSSP; P08659; 1LCI. DR SGD; S0000426; FAT2. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00455; AMP_BINDING; 1. KW Ligase; Peroxisome. FT NP_BIND 190 207 AMP (BY SIMILARITY). FT SITE 541 543 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 543 AA; 60488 MW; 2BA18B77D10D62F2 CRC64; MTSAATVTAS FNDTFSVSDN VAVIVPETDT QVTYRDLSHM VGHFQTMFTN PNSPLYGAVF RQDTVAISMR NGLEFIVAFL GATMDAKIGA PLNPNYKEKE FNFYLNDLKS KAICVPKGTT KLQSSEILKS ASTFGCFIVE LAFDATRFRV EYDIYSPEDN YKRVIYRSLN NAKFVNTNPV KFPGFARSSD VALILHTSGT TSTPKTVPLL HLNIVRSTLN IANTYKLTPL DRSYVVMPLF HVHGLIGVLL STFRTQGSVV VPDGFHPKLF WDQFVKYNCN WFSCVPTISM IMLNMPKPNP FPHIRFIRSC SSALAPATFH KLEKEFNAPV LEAYAMTEAS HQMTSNNLPP GKRKPGTVGQ PQGVTVVILD DNDNVLPPGK VGEVSIRGEN VTLGYANNPK ANKENFTKRE NYFRTGDQGY FDPEGFLVLT GRIKELINRG GEKISPIELD GIMLSHPKID EAVAFGVPDD MYGQVVQAAI VLKKGEKMTY EELVNFLKKH LASFKIPTKV YFVDKLPKTA TGKIQRRVIA ETFAKSSRNK SKL // ID FOX2_CANTR STANDARD; PRT; 906 AA. AC P22414; DT 01-AUG-1991 (Rel. 19, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Peroxisomal hydratase-dehydrogenase-epimerase (HDE) (Multifunctional DE beta-oxidation protein) (MFP) [Includes: 2-enoyl-CoA hydratase DE (EC 4.2.1.-); D-3-hydroxyacyl CoA dehydrogenase (EC 1.1.1.-)]. OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5482; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 20336 / PK233; RX MEDLINE=89172062; PubMed=3267241; RA Nuttley W.M., Aitchison J.D., Rachubinski R.A.; RT "cDNA cloning and primary structure determination of the peroxisomal RT trifunctional enzyme hydratase-dehydrogenase-epimerase from the yeast RT Candida tropicalis pK233."; RL Gene 69:171-180(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 20336 / PK233; RX MEDLINE=92039009; PubMed=1937002; RA Aitchison J.D., Sloots J.A., Nuttley W.M., Rachubinski R.A.; RT "Glucose-responsive and oleic acid-responsive elements in the gene RT encoding the peroxisomal trifunctional enzyme of Candida RT tropicalis."; RL Gene 105:129-134(1991). RN [3] RP SIMILARITY TO SHORT CHAIN DEHYDROGENASES OF N-TERMINAL DOMAIN. RX MEDLINE=90367890; PubMed=2394320; RA Baker M.E.; RT "A common ancestor for Candida tropicalis and dehydrogenases that RT synthesize antibiotics and steroids."; RL FASEB J. 4:3028-3032(1990). CC -!- FUNCTION: SECOND TRIFUNCTIONAL ENZYME ACTING ON THE BETA-OXIDATION CC PATHWAY FOR FATTY ACIDS, POSSESSING HYDRATASE-DEHYDROGENASE- CC EPIMERASE ACTIVITIES. CONVERTS TRANS-2-ENOYL-COA VIA D-3- CC HYDROXYACYL-COA TO 3-KETOACYL-COA. CC -!- PATHWAY: BETA-OXIDATION PATHWAY. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- INDUCTION: BY GROWTH ON N-ALKANES OR FATTY ACIDS. CC -!- DOMAIN: CONTAINS TWO SDR DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22765; AAA62847.1; -. DR EMBL; X57854; CAA40989.1; -. DR PIR; JT0350; JT0350. DR HSSP; P25529; 1AHH. DR InterPro; IPR002198; ADH_short. DR InterPro; IPR002347; Adh_short_C2. DR InterPro; IPR002539; MaoC_dehydratas. DR Pfam; PF00106; adh_short; 2. DR Pfam; PF01575; MaoC_dehydratas; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 2. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Multifunctional enzyme; Oxidoreductase; NAD; KW Lyase; Isomerase; Peroxisome; Repeat. FT DOMAIN 5 228 SHORT-CHAIN DEHYDROGENASE LIKE 1. FT DOMAIN 319 532 SHORT-CHAIN DEHYDROGENASE LIKE 2. FT SITE 904 906 MICROBODY TARGETING SIGNAL (POTENTIAL). FT NP_BIND 12 36 NAD (BY SIMILARITY). FT ACT_SITE 163 163 BY SIMILARITY. FT NP_BIND 326 350 NAD (BY SIMILARITY). FT ACT_SITE 467 467 BY SIMILARITY. FT CONFLICT 540 540 F -> S (IN REF. 1). SQ SEQUENCE 906 AA; 99469 MW; 65AB88C8671C967B CRC64; MSPVDFKDKV VIITGAGGGL GKYYSLEFAK LGAKVVVNDL GGALNGQGGN SKAADVVVDE IVKNGGVAVA DYNNVLDGDK IVETAVKNFG TVHVIINNAG ILRDASMKKM TEKDYKLVID VHLNGAFAVT KAAWPYFQKQ KYGRIVNTSS PAGLYGNFGQ ANYASAKSAL LGFAETLAKE GAKYNIKANA IAPLARSRMT ESILPPPMLE KLGPEKVAPL VLYLSSAENE LTGQFFEVAA GFYAQIRWER SGGVLFKPDQ SFTAEVVAKR FSEILDYDDS RKPEYLKNQY PFMLNDYATL TNEARKLPAN DASGAPTVSL KDKVVLITGA GAGLGKEYAK WFAKYGAKVV VNDFKDATKT VDEIKAAGGE AWPDQHDVAK DSEAIIKNVI DKYGTIDILV NNAGILRDRS FAKMSKQEWD SVQQVHLIGT FNLSRLAWPY FVEKQFGRII NITSTSGIYG NFGQANYSSS KAGILGLSKT MAIEGAKNNI KVNIVAPHAE TAMTLTIFRE QDKNLYHADQ VAPLLVYLGT DDVPVTGETF EIGGGWIGNT RWQRAKGAVS HDEHTTVEFI KEHLNEITDF TTDTENPKST TESSMAILSA VGGDDDDDDE DEEEDEGDEE EDEEDEEEDD PVWRFDDRDV ILYNIALGAT TKQLKYVYEN DSDFQVIPTF GHLITFNSGK SQNSFAKLLR NFNPMLLLHG EHYLKVHSWP PPTEGEIKTT FEPIATTPKG TNVVIVHGSK SVDNKSGELI YSNEATYFIR NCQADNKVYA DRPAFATNQF LAPKRAPDYQ VDVPVSEDLA ALYRLSGDRN PLHIDPNFAK GAKFPKPILH GMCTYGLSAK ALIDKFGMFN EIKARFTGIV FPGETLRVLA WKESDDTIVF QTHVVDRGTI AINNAAIKLV GDKAKI // ID FOX2_YEAST STANDARD; PRT; 900 AA. AC Q02207; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal hydratase-dehydrogenase-epimerase (HDE) (Multifunctional DE beta-oxidation protein) (MFP) [Includes: 2-enoyl-CoA hydratase DE (EC 4.2.1.-); D-3-hydroxyacyl CoA dehydrogenase (EC 1.1.1.-)]. GN FOX2 OR YKR009C OR YK108. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=93070612; PubMed=1441752; RA Duesterhoeft A., Philippsen P.; RT "DNA sequencing and analysis of a 24.7 kb segment encompassing RT centromere CEN11 of Saccharomyces cerevisiae reveals nine previously RT unknown open reading frames."; RL Yeast 8:749-759(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92202210; PubMed=1551874; RA Hiltunen J.K., Wenzel B., Beyer A., Erdmann R., Fossa A., Kunau W.H.; RT "Peroxisomal multifunctional beta-oxidation protein of Saccharomyces RT cerevisiae. Molecular analysis of the fox2 gene and gene product."; RL J. Biol. Chem. 267:6646-6653(1992). CC -!- FUNCTION: SECOND TRIFUNCTIONAL ENZYME ACTING ON THE BETA-OXIDATION CC PATHWAY FOR FATTY ACIDS, POSSESSING HYDRATASE-DEHYDROGENASE- CC EPIMERASE ACTIVITIES. CONVERTS TRANS-2-ENOYL-COA VIA D-3- CC HYDROXYACYL-COA TO 3-KETOACYL-COA. CC -!- PATHWAY: BETA-OXIDATION PATHWAY. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- DOMAIN: CONTAINS TWO SDR DOMAINS. CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86456; AAA34779.1; -. DR EMBL; X65124; CAA46243.1; -. DR EMBL; Z28234; CAA82079.1; -. DR PIR; S25322; S25322. DR HSSP; P25529; 1AHH. DR SGD; S0001717; FOX2. DR InterPro; IPR002198; ADH_short. DR InterPro; IPR002347; Adh_short_C2. DR InterPro; IPR002539; MaoC_dehydratas. DR Pfam; PF00106; adh_short; 2. DR Pfam; PF01575; MaoC_dehydratas; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 2. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Fatty acid metabolism; Multifunctional enzyme; Oxidoreductase; NAD; KW Lyase; Isomerase; Peroxisome; Repeat. FT DOMAIN 6 230 SHORT-CHAIN DEHYDROGENASE LIKE 1. FT DOMAIN 319 535 SHORT-CHAIN DEHYDROGENASE LIKE 2. FT SITE 898 900 MICROBODY TARGETING SIGNAL (POTENTIAL). FT NP_BIND 13 37 NAD (BY SIMILARITY). FT ACT_SITE 165 165 BY SIMILARITY. FT NP_BIND 326 350 NAD (BY SIMILARITY). FT ACT_SITE 469 469 BY SIMILARITY. SQ SEQUENCE 900 AA; 98703 MW; 66FFD0D49C673788 CRC64; MPGNLSFKDR VVVITGAGGG LGKVYALAYA SRGAKVVVND LGGTLGGSGH NSKAADLVVD EIKKAGGIAV ANYDSVNENG EKIIETAIKE FGRVDVLINN AGILRDVSFA KMTEREFASV VDVHLTGGYK LSRAAWPYMR SQKFGRIINT ASPAGLFGNF GQANYSAAKM GLVGLAETLA KEGAKYNINV NSIAPLARSR MTENVLPPHI LKQLGPEKIV PLVLYLTHES TKVSNSIFEL AAGFFGQLRW ERSSGQIFNP DPKTYTPEAI LNKWKEITDY RDKPFNKTQH PYQLSDYNDL ITKAKKLPPN EQGSVKIKSL CNKVVVVTGA GGGLGKSHAI WFARYGAKVV VNDIKDPFSV VEEINKLYGE GTAIPDSHDV VTEAPLIIQT AISKFQRVDI LVNNAGILRD KSFLKMKDEE WFAVLKVHLF STFSLSKAVW PIFTKQKSGF IINTTSTSGI YGNFGQANYA AAKAAILGFS KTIALEGAKR GIIVNVIAPH AETAMTKTIF SEKELSNHFD ASQVSPLVVL LASEELQKYS GRRVIGQLFE VGGGWCGQTR WQRSSGYVSI KETIEPEEIK ENWNHITDFS RNTINPSSTE ESSMATLQAV QKAHSSKELD DGLFKYTTKD CILYNLGLGC TSKELKYTYE NDPDFQVLPT FAVIPFMQAT ATLAMDNLVD NFNYAMLLHG EQYFKLCTPT MPSNGTLKTL AKPLQVLDKN GKAALVVGGF ETYDIKTKKL IAYNEGSFFI RGAHVPPEKE VRDGKRAKFA VQNFEVPHGK VPDFEAEIST NKDQAALYRL SGDFNPLHID PTLAKAVKFP TPILHGLCTL GISAKALFEH YGPYEELKVR FTNVVFPGDT LKVKAWKQGS VVVFQTIDTT RNVIVLDNAA VKLSQAKSKL // ID GOX1_ARATH STANDARD; PRT; 367 AA. AC Q9LRS0; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Probable (S)-2-hydroxy-acid oxidase, peroxisomal 1 (EC 1.1.3.15) DE (Glycolate oxidase 1) (GOX 1) (Short chain alpha-hydroxy acid oxidase DE 1). GN AT3G14415 OR MLN21.20. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20277480; PubMed=10819329; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN (BY SIMILARITY). CC -!- PATHWAY: SECOND REACTION OF THE PHOTORESPIRATORY PATHWAY CC (GLYCOLATE PATHWAY). CC -!- SUBUNIT: HOMOTETRAMER OR HOMOOCTAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB028617; BAB01333.1; -. DR EMBL; AB022220; BAB01333.1; JOINED. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR InterPro; IPR000865; Microbodies_C. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; FALSE_NEG. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway; KW Photorespiration. FT ACT_SITE 24 24 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 129 129 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 254 254 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 257 257 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 365 367 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 367 AA; 40306 MW; C0B0F9B083F1B6E6 CRC64; MEITNVTEYD AIAKAKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR ILIDVNKIDM ATTVLGFKIS MPIMVAPTAF QKMAHPDGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG PGIRFFQLYV YKNRKVVEQL VRRAEKAGFK AIALTVDTPR LGRRESDIKN RFTLPPNLTL KNFEGLDLGK MDEANDSGLA SYVAGQIDRT LSWKDIQWLQ TITNMPILVK GVLTGEDARI AIQAGAAGII VSNHGARQLD YVPATISALE EVVKATQGRV PVFLDGGVRR GTDVFKALAL GASGIFIGRP VVFALAAEGE AGVKKVLQML RDEFELTMAL SGCRSLSEIT RNHIVTEWDT PRHLPRL // ID GOX2_ARATH STANDARD; PRT; 367 AA. AC Q9LRR9; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Probable (S)-2-hydroxy-acid oxidase, peroxisomal 2 (EC 1.1.3.15) DE (Glycolate oxidase 2) (GOX 2) (Short chain alpha-hydroxy acid oxidase DE 2). GN AT3G14420 OR MAO2.2. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20277480; PubMed=10819329; RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC RT clones."; RL DNA Res. 7:131-135(2000). CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN (BY SIMILARITY). CC -!- PATHWAY: SECOND REACTION OF THE PHOTORESPIRATORY PATHWAY CC (GLYCOLATE PATHWAY). CC -!- SUBUNIT: HOMOTETRAMER OR HOMOOCTAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB028617; BAB01334.1; -. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway; KW Photorespiration. FT ACT_SITE 24 24 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 129 129 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 254 254 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 257 257 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 365 367 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 367 AA; 40341 MW; B107AD7AC983A04C CRC64; MEITNVTEYD AIAKQKLPKM VYDYYASGAE DQWTLQENRN AFARILFRPR ILIDVSKIDM TTTVLGFKIS MPIMVAPTAM QKMAHPDGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG PGIRFFQLYV YKNRNVVEQL VRRAERAGFK AIALTVDTPR LGRRESDIKN RFTLPPNLTL KNFEGLDLGK MDEANDSGLA SYVAGQIDRT LSWKDVQWLQ TITKLPILVK GVLTGEDARI AIQAGAAGII VSNHGARQLD YVPATISALE EVVKATQGRI PVFLDGGVRR GTDVFKALAL GASGIFIGRP VVFSLAAEGE AGVRKVLQML RDEFELTMAL SGCRSLKEIS RNHITTEWDT PRPSARL // ID GOX_SPIOL STANDARD; PRT; 369 AA. AC P05414; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE (S)-2-hydroxy-acid oxidase, peroxisomal (EC 1.1.3.15) (Glycolate DE oxidase) (GOX) (Short chain alpha-hydroxy acid oxidase). OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllidae; Caryophyllales; Chenopodiaceae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88058933; PubMed=2824469; RA Volokita M., Somerville C.R.; RT "The primary structure of spinach glycolate oxidase deduced from the RT DNA sequence of a cDNA clone."; RL J. Biol. Chem. 262:15825-15828(1987). RN [2] RP SEQUENCE. RX MEDLINE=88225066; PubMed=3286256; RA Cederlund E., Lindqvist Y., Soederlund G., Braenden C.-I., RA Joernvall H.; RT "Primary structure of glycolate oxidase from spinach."; RL Eur. J. Biochem. 173:523-530(1988). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=90040713; PubMed=2681790; RA Lindqvist Y.; RT "Refined structure of spinach glycolate oxidase at 2-A resolution."; RL J. Mol. Biol. 209:151-166(1989). RN [4] RP ACTIVE SITE. RX MEDLINE=89123500; PubMed=2644287; RA Lindqvist Y., Braenden C.-I.; RT "The active site of spinach glycolate oxidase."; RL J. Biol. Chem. 264:3624-3628(1989). CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- PATHWAY: SECOND REACTION OF THE PHOTORESPIRATORY PATHWAY CC (GLYCOLATE PATHWAY). CC -!- SUBUNIT: HOMOTETRAMER OR HOMOOCTAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03492; AAA34030.1; -. DR PIR; A28496; OXSPH. DR PIR; S00621; S00621. DR PDB; 1GOX; 15-OCT-89. DR PDB; 1AL7; 12-NOV-97. DR PDB; 1AL8; 17-SEP-97. DR PDB; 1GYL; 31-MAR-95. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway; KW Photorespiration; 3D-structure; Acetylation. FT MOD_RES 1 1 ACETYLATION. FT ACT_SITE 24 24 SUBSTRATE BINDING. FT ACT_SITE 129 129 SUBSTRATE BINDING. FT ACT_SITE 254 254 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS. FT ACT_SITE 257 257 SUBSTRATE BINDING. FT SITE 367 369 MICROBODY TARGETING SIGNAL (POTENTIAL). FT TURN 6 7 FT HELIX 8 16 FT HELIX 19 26 FT TURN 30 31 FT HELIX 33 44 FT STRAND 45 47 FT STRAND 59 59 FT STRAND 62 64 FT TURN 65 66 FT STRAND 67 69 FT STRAND 73 75 FT HELIX 81 83 FT TURN 84 84 FT TURN 86 87 FT HELIX 88 98 FT TURN 99 100 FT STRAND 103 105 FT TURN 107 108 FT HELIX 113 117 FT TURN 118 119 FT STRAND 124 128 FT STRAND 131 131 FT HELIX 134 146 FT TURN 147 148 FT STRAND 151 155 FT HELIX 165 169 FT TURN 170 171 FT TURN 176 177 FT HELIX 181 183 FT HELIX 199 205 FT TURN 206 206 FT STRAND 207 207 FT TURN 209 210 FT HELIX 213 222 FT STRAND 227 230 FT HELIX 235 243 FT TURN 244 245 FT STRAND 248 251 FT HELIX 254 256 FT TURN 257 257 FT TURN 260 261 FT HELIX 265 275 FT TURN 276 278 FT STRAND 282 285 FT HELIX 291 300 FT TURN 301 301 FT STRAND 304 307 FT HELIX 309 341 FT TURN 342 342 FT STRAND 345 345 FT TURN 346 348 FT HELIX 351 353 FT STRAND 354 356 FT TURN 357 358 SQ SEQUENCE 369 AA; 40285 MW; 892F1B3D0C1B48E0 CRC64; MEITNVNEYE AIAKQKLPKM VYDYYASGAE DQWTLAENRN AFSRILFRPR ILIDVTNIDM TTTILGFKIS MPIMIAPTAM QKMAHPEGEY ATARAASAAG TIMTLSSWAT SSVEEVASTG PGIRFFQLYV YKDRNVVAQL VRRAERAGFK AIALTVDTPR LGRREADIKN RFVLPPFLTL KNFEGIDLGK MDKANDSGLS SYVAGQIDRS LSWKDVAWLQ TITSLPILVK GVITAEDARL AVQHGAAGII VSNHGARQLD YVPATIMALE EVVKAAQGRI PVFLDGGVRR GTDVFKALAL GAAGVFIGRP VVFSLAAEGE AGVKKVLQMM RDEFELTMAL SGCRSLKEIS RSHIAADWDG PSSRAVARL // ID HAO1_HUMAN STANDARD; PRT; 370 AA. AC Q9UJM8; Q9UPZ0; Q9Y3I7; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hydroxyacid oxidase 1 (EC 1.1.3.15) (HAOX1) (Glycolate oxidase) (GOX). GN HAO1 OR HAOX1 OR GOX1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=20435306; PubMed=10978532; RA Williams E.L., Cregeen D.P., Rumsby G.; RT "Identification and expression of a cDNA for human glycolate RT oxidase."; RL Biochim. Biophys. Acta 1493:246-248(2000). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20239903; PubMed=10777549; RA Jones J.M., Morrell J.C., Gould S.J.; RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three RT human peroxisomal 2-hydroxy acid oxidases."; RL J. Biol. Chem. 275:12590-12597(2000). RN [3] RP SEQUENCE FROM N.A. RA Stavrides G.S., Huckle E.J., Deloukas P.; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RA Watanabe T.; RT "Isolation and characterization of a novel human liver-specific gene RT homologous to the plant glycolate oxidase by the differential display RT method."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RA Clark G.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: HAS 2-HYDROXYACID OXIDASE ACTIVITY. MOST ACTIVE ON THE CC 2-CARBON SUBSTRATE GLYCOLATE, BUT IS ALSO ACTIVE ON 2-HYDROXY CC FATTY ACIDS. CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- PATHWAY: SECOND REACTION OF THE GLYCOLATE PATHWAY (KNOWN AS THE CC PHOTORESPIRATORY PATHWAY IN PLANT). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: LIVER. CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AL121739; CAB57329.1; -. DR EMBL; AF244134; AAF63219.1; -. DR EMBL; AF231916; AAF40199.1; -. DR EMBL; AB024079; BAA82872.1; -. DR EMBL; AL021879; CAC34364.1; -. DR HSSP; P05414; 1GOX. DR MIM; 605023; -. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway. FT ACT_SITE 26 26 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 132 132 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 260 260 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 263 263 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 368 370 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 370 AA; 40924 MW; C683C6F7CB5FD323 CRC64; MLPRLICIND YEQHAKSVLP KSIYDYYRSG ANDEETLADN IAAFSRWKLY PRMLRNVAET DLSTSVLGQR VSMPICVGAT AMQRMAHVDG ELATVRACQS LGTGMMLSSW ATSSIEEVAE AGPEALRWLQ LYIYKDREVT KKLVRQAEKM GYKAIFVTVD TPYLGNRLDD VRNRFKLPPQ LRMKNFETST LSFSPEENFG DDSGLAAYVA KAIDPSISWE DIKWLRRLTS LPIVAKGILR GDDAREAVKH GLNGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV LKALALGAKA VFVGRPIVWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ NVKVIDKTLV RKNPLAVSKI // ID HAO1_MOUSE STANDARD; PRT; 370 AA. AC Q9WU19; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hydroxyacid oxidase 1 (EC 1.1.3.15) (HAOX1) (Glycolate oxidase) (GOX). GN HAO1 OR HAO-1 OR GOX1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=99107899; PubMed=9891009; RA Kohler S.A., Menotti E., Kuhn L.C.; RT "Molecular cloning of mouse glycolate oxidase. High evolutionary RT conservation and presence of an iron-responsive element-like sequence RT in the mRNA."; RL J. Biol. Chem. 274:2401-2407(1999). CC -!- FUNCTION: HAS 2-HYDROXYACID OXIDASE ACTIVITY. MOST ACTIVE ON THE CC 2-CARBON SUBSTRATE GLYCOLATE, BUT IS ALSO ACTIVE ON 2-HYDROXY CC FATTY ACIDS. CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- PATHWAY: SECOND REACTION OF THE GLYCOLATE PATHWAY (KNOWN AS THE CC PHOTORESPIRATORY PATHWAY IN PLANT). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: LIVER. CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF104312; AAD25332.1; -. DR HSSP; P05414; 1AL8. DR MGD; MGI:96011; Hao1. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome; Glycolate pathway. FT ACT_SITE 26 26 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 132 132 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 260 260 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 263 263 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 368 370 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 370 AA; 41001 MW; 97339211AF9FC19C CRC64; MLPRLVCISD YEQHVRSVLQ KSVYDYYRSG ANDQETLADN IQAFSRWKLY PRMLRNVADI DLSTSVLGQR VSMPICVGAT AMQCMAHVDG ELATVRACQT MGTGMMLSSW ATSSIEEVAE AGPEALRWMQ LYIYKDREIS RQIVKRAEKQ GYKAIFVTVD TPYLGNRIDD VRNRFKLPPQ LRMKNFETND LAFSPKGNFG DNSGLAEYVA QAIDPSLSWD DITWLRRLTS LPIVVKGILR GDDAKEAVKH GVDGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV LKALALGAKA VFVGRPIIWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ NVKVIDKTLV RKNPLAVSKI // ID HAO2_HUMAN STANDARD; PRT; 351 AA. AC Q9NYQ3; Q9UJS6; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hydroxyacid oxidase 2 (EC 1.1.3.15) (HAOX2) ((S)-2-hydroxy-acid DE oxidase, peroxisomal) (Long chain alpha-hydroxy acid oxidase) (Long- DE chain L-2-hydroxy acid oxidase). GN HAO2 OR HAOX2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20239903; PubMed=10777549; RA Jones J.M., Morrell J.C., Gould S.J.; RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three RT human peroxisomal 2-hydroxy acid oxidases."; RL J. Biol. Chem. 275:12590-12597(2000). RN [2] RP SEQUENCE FROM N.A. RA Spielbauer B., Conzelmann E.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RA Donnelly S.; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE OXIDATION OF L-ALPHA-HYDROXY ACIDS AS WELL CC AS, MORE SLOWLY, THAT OF L-ALPHA-AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: LIVER AND KIDNEY. CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF231917; AAF40200.1; -. DR EMBL; AF203975; AAF14000.1; -. DR EMBL; AL359553; CAC19798.1; -. DR HSSP; P05414; 1GOX. DR MIM; 605176; -. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome. FT ACT_SITE 24 24 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 130 130 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 246 246 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 249 249 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 349 351 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 80 80 F -> Y (IN REF. 2). FT CONFLICT 292 294 LGA -> HED (IN REF. 2). SQ SEQUENCE 351 AA; 38838 MW; 7330DE44E282947D CRC64; MSLVCLTDFQ AHAREQLSKS TRDFIEGGAD DSITRDDNIA AFKRIRLRPR YLRDVSEVDT RTTIQGEEIS APICIAPTGF HCLVWPDGEM STARAAQAAG ICYITSTFAS CSLEDIVIAA PEGLRWFQLY VHPDLQLNKQ LIQRVESLGF KALVITLDTP VCGNRRHDIR NQLRRNLTLT DLQSPKKGNA IPYFQMTPIS TSLCWNDLSW FQSITRLPII LKGILTKEDA ELAVKHNVQG IIVSNHGGRQ LDEVLASIDA LTEVVAAVKG KIEVYLDGGV RTGNDVLKAL ALGAKCIFLG RPILWGLACK GEHGVKEVLN ILTNEFHTSM ALTGCRSVAE INRNLVQFSR L // ID HAO3_HUMAN STANDARD; PRT; 353 AA. AC Q9NYQ2; Q9JI00; Q9JHS7; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hydroxyacid oxidase 3 (EC 1.1.3.15) (HAOX3) ((S)-2-hydroxy-acid DE oxidase, peroxisomal) (Medium chain alpha-hydroxy acid oxidase) DE (Medium-chain L-2-hydroxy acid oxidase). GN HAO3 OR HAOX3. OS Homo sapiens (Human), and OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 10090; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=20239903; PubMed=10777549; RA Jones J.M., Morrell J.C., Gould S.J.; RT "Identification and characterization of HAOX1, HAOX2, and HAOX3, three RT human peroxisomal 2-hydroxy acid oxidases."; RL J. Biol. Chem. 275:12590-12597(2000). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RA Spielbauer B., Conzelmann E.; RT "Mus musculus long-chain L-2-hydroxy acid oxidase."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RA Van Veldhoven P.P.; RT "Search for PTS1-containing protein in mammals."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: HAS 2-HYDROXYACID OXIDASE ACTIVITY. MOST ACTIVE ON CC MEDIUM-CHAIN SUBSTRATES. CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: PANCREAS. CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF231918; AAF40201.1; -. DR EMBL; AF272947; AAF81795.1; -. DR EMBL; AJ251820; CAB96380.1; -. DR MIM; 605177; -. DR MGD; MGI:1860477; Hao3. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome. FT ACT_SITE 24 24 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 130 130 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 248 248 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 251 251 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 351 353 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 164 164 N -> H (IN REF. 3). SQ SEQUENCE 353 AA; 38699 MW; 0604D529F69DE3C7 CRC64; MSLLCLADFK AQAQKQLSKT SWDFIEGEAD DGITYNDNLA AFRRIRLRPR YLRDVSKIDT RTTIQGQEIN APICISPTAF HSIAWADGEK STAKAAQKAN ICYVISSYAS YTVEDIVAAA PGGLHWFQLY VQPDWDINKQ MVQRIEALGF KALVVTVDAP VLGNRRGNKR SLLDLEANIK LKDLRSPGES KSGLPTPLSM PSSSSCWNDL PLLQSMTRLP IILKGILTKE DAELAVKHNI RGIIVSNHGG RQLDEVPASI DALREVVAAV NGKIEVYMDG GVRTGNDVLK ALALGARCIF LGRPIIWGLA CKGEDGVKEV LDILKEELHT CMALSGCRSV AEISPDLIQF SRL // ID HAO3_RAT STANDARD; PRT; 352 AA. AC Q07523; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Hydroxyacid oxidase 3 (EC 1.1.3.15) (HAOX3) ((S)-2-hydroxy-acid DE oxidase, peroxisomal) (Long chain alpha-hydroxy acid oxidase) (Long- DE chain L-2-hydroxy acid oxidase). GN HAO3 OR HAOX3. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Kidney; RX MEDLINE=93285140; PubMed=8508789; RA Belmouden A., Le K.H.D., Lederer F., Garchon H.J.; RT "Molecular cloning and nucleotide sequence of cDNA encoding rat RT kidney long-chain L-2-hydroxy acid oxidase. Expression of the RT catalytically active recombinant protein as a chimaera."; RL Eur. J. Biochem. 214:17-25(1993). RN [2] RP SEQUENCE. RC TISSUE=Kidney; RX MEDLINE=92041948; PubMed=1939137; RA Le K.H.D., Lederer F.; RT "Amino acid sequence of long chain alpha-hydroxy acid oxidase from RT rat kidney, a member of the family of FMN-dependent alpha-hydroxy RT acid-oxidizing enzymes."; RL J. Biol. Chem. 266:20877-20881(1991). RN [3] RP SEQUENCE OF 1-40, AND CHARACTERIZATION. RX MEDLINE=89088098; PubMed=3061453; RA Urban P., Chirat I., Lederer F.; RT "Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic RT comparison with flavocytochrome b2 from baker's yeast."; RL Biochemistry 27:7365-7371(1988). CC -!- FUNCTION: CATALYZES THE OXIDATION OF L-ALPHA-HYDROXY ACIDS AS WELL CC AS, MORE SLOWLY, THAT OF L-ALPHA-AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: (S)-2-HYDROXY-ACID + O(2) = 2-OXO ACID + CC H(2)O(2). CC -!- COFACTOR: FMN. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE FMN-DEPENDENT ALPHA-HYDROXY ACID CC DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67156; CAA47629.1; -. DR HSSP; P05414; 1GYL. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR000262; FMN_hydroxy_acid_dh. DR Pfam; PF01070; FMN_dh; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH; 1. KW Oxidoreductase; Flavoprotein; FMN; Peroxisome. FT INIT_MET 0 0 FT ACT_SITE 23 23 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 129 129 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 247 247 REMOVES THE SUBSTRATE ALPHA-PROTON AS THE FT FIRST STEP IN CATALYSIS (BY SIMILARITY). FT ACT_SITE 250 250 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 350 352 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 352 AA; 39070 MW; BC082E7081C5E7D1 CRC64; PLVCLADFKA HAQKQLSKTS WDFIEGEADD GITYSENIAA FKRIRLRPRY LRDMSKVDTR TTIQGQEISA PICISPTAFH SIAWPDGEKS TARAAQEANI CYVISSYASY SLEDIVAAAP EGFRWFQLYM KSDWDFNKQM VQRAEALGFK ALVITIDTPV LGNRRRDKRN QLNLEANILL KDLRALKEEK PTQSVPVSFP KASFCWNDLS LLQSITRLPI ILKGILTKED AELAMKHNVQ GIVVSNHGGR QLDEVSASID ALREVVAAVK GKIEVYMDGG VRTGTDVLKA LALGARCIFL GRPILWGLAC KGEDGVKEVL DILTAELHRC MTLSGCQSVA EISPDLIQFS RL // ID HYES_HUMAN STANDARD; PRT; 554 AA. AC P34913; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Soluble epoxide hydrolase (SEH) (EC 3.3.2.3) (Epoxide hydratase) DE (Cytosolic epoxide hydrolase) (CEH). GN EPHX2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=93343630; PubMed=8342951; RA Beetham J.K., Tian T., Hammock B.D.; RT "cDNA cloning and expression of a soluble epoxide hydrolase from RT human liver."; RL Arch. Biochem. Biophys. 305:197-201(1993). CC -!- FUNCTION: THIS ENZYME ACTS ON EPOXIDES (ALKENE OXIDES, OXIRANES) CC AND ARENE OXIDES. PLAYS A ROLE IN XENOBIOTIC METABOLISM CC BY DEGRADING POTENTIAL TOXIC EPOXIDES. ALSO DETERMINES STEADY- CC STATE LEVELS OF PHYSIOLOGICAL MEDIATORS. CC -!- CATALYTIC ACTIVITY: AN EPOXIDE + H(2)O = A GLYCOL. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND PEROXISOMAL. CC -!- INDUCTION: BY COMPOUNDS THAT CAUSE PEROXISOME PROLIFERATION CC SUCH AS CLOFIBRATE, TIADENOL AND FENOFIBRATE. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05779; AAA02756.1; -. DR PIR; S35587; S35587. DR MIM; 132811; -. DR InterPro; IPR003089; AB_hydrolase. DR InterPro; IPR000073; Abhydrolase. DR InterPro; IPR000639; Epox_hydrlse. DR InterPro; IPR000379; Est_lip_thioest_actsite. DR InterPro; IPR001454; Hydrolase. DR Pfam; PF00561; abhydrolase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00412; EPOXHYDRLASE. DR PRINTS; PR00413; HADHALOGNASE. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Hydrolase; Peroxisome; Detoxification; KW Aromatic hydrocarbons catabolism. FT ACT_SITE 333 333 BY SIMILARITY. FT ACT_SITE 495 495 BY SIMILARITY. FT ACT_SITE 523 523 BY SIMILARITY. FT SITE 552 554 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 554 AA; 62643 MW; EF729FE3D7425A95 CRC64; MTLRGAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL HFVELGWPAV CLCHGFPESW YSWRYQIPAL AQAGYRVLAM DMKGYGESSA PPEIEEYCME VLCKEMVTFL DKLGLSQAVF IGHDWGGMLV WYMALFYPER VRAVASLNTP FIPANPNMSP LESIKANPVF DYQLYFQEPG VAEAELEQNL SRTFKSLFRA SDESVLSMHK VCEAGGLFVN SPEEPSLSRM VTEEEIQFYV QQFKKSGFRG PLNWYRNMER NWKWACKSLG RKILIPALMV TAEKDFVLVP QMSQHMEDWI PHLKRGHIED CGHWTQMDKP TEVNQILIKW LDSDARNPPV VSKM // ID HYES_MOUSE STANDARD; PRT; 554 AA. AC P34914; DT 01-FEB-1994 (Rel. 28, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Soluble epoxide hydrolase (SEH) (EC 3.3.2.3) (Epoxide hydratase) DE (Cytosolic epoxide hydrolase) (CEH). GN EPHX2 OR EPH2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=93352558; PubMed=8349642; RA Grant D.F., Storms D.H., Hammock B.D.; RT "Molecular cloning and expression of murine liver soluble epoxide RT hydrolase."; RL J. Biol. Chem. 268:17628-17633(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NMRI; RX MEDLINE=96307695; PubMed=8750907; RA Johansson C., Stark A., Sandberg M., Ek B., Rask L., Meijer J.; RT "Tissue specific basal expression of soluble murine epoxide hydrolase RT and effects of clofibrate on the mRNA levels in extrahepatic tissues RT and liver."; RL Arch. Toxicol. 70:61-63(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RC TISSUE=Liver; RX MEDLINE=99415911; PubMed=10485878; RA Argiriadi M.A., Morisseau C., Hammock B.D., Christianson D.W.; RT "Detoxification of environmental mutagens and carcinogens: structure, RT mechanism, and evolution of liver epoxide hydrolase."; RL Proc. Natl. Acad. Sci. U.S.A. 96:10637-10642(1999). CC -!- FUNCTION: THIS ENZYME ACTS ON EPOXIDES (ALKENE OXIDES, OXIRANES) CC AND ARENE OXIDES. PLAYS A ROLE IN XENOBIOTIC METABOLISM CC BY DEGRADING POTENTIAL TOXIC EPOXIDES. ALSO DETERMINES STEADY- CC STATE LEVELS OF PHYSIOLOGICAL MEDIATORS. CC -!- CATALYTIC ACTIVITY: AN EPOXIDE + H(2)O = A GLYCOL. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND PEROXISOMAL. CC -!- INDUCTION: BY COMPOUNDS THAT CAUSE PEROXISOME PROLIFERATION CC SUCH AS CLOFIBRATE, TIADENOL AND FENOFIBRATE. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05781; AAA37555.1; -. DR EMBL; Z37107; CAA85471.1; -. DR PIR; A47504; A47504. DR PDB; 1CQZ; 19-NOV-99. DR PDB; 1CR6; 19-NOV-99. DR SWISS-2DPAGE; P34914; MOUSE. DR MGD; MGI:99500; Ephx2. DR InterPro; IPR003089; AB_hydrolase. DR InterPro; IPR000073; Abhydrolase. DR InterPro; IPR000639; Epox_hydrlse. DR InterPro; IPR000379; Est_lip_thioest_actsite. DR InterPro; IPR001454; Hydrolase. DR Pfam; PF00561; abhydrolase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00412; EPOXHYDRLASE. DR PRINTS; PR00413; HADHALOGNASE. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Hydrolase; Peroxisome; Detoxification; KW Aromatic hydrocarbons catabolism; 3D-structure. FT ACT_SITE 333 333 BY SIMILARITY. FT ACT_SITE 495 495 BY SIMILARITY. FT ACT_SITE 523 523 BY SIMILARITY. FT SITE 552 554 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 77 77 A -> T (IN REF. 2). SQ SEQUENCE 554 AA; 62515 MW; 2F3A3F7DACE47C93 CRC64; MALRVAAFDL DGVLALPSIA GAFRRSEEAL ALPRDFLLGA YQTEFPEGPT EQLMKGKITF SQWVPLMDES YRKSSKACGA NLPENFSISQ IFSQAMAARS INRPMLQAAI ALKKKGFTTC IVTNNWLDDG DKRDSLAQMM CELSQHFDFL IESCQVGMIK PEPQIYNFLL DTLKAKPNEV VFLDDFGSNL KPARDMGMVT ILVHNTASAL RELEKVTGTQ FPEAPLPVPC NPNDVSHGYV TVKPGIRLHF VEMGSGPALC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP PEIEEYAMEL LCKEMVTFLD KLGIPQAVFI GHDWAGVMVW NMALFYPERV RAVASLNTPF MPPDPDVSPM KVIRSIPVFN YQLYFQEPGV AEAELEKNMS RTFKSFFRAS DETGFIAVHK ATEIGGILVN TPEDPNLSKI TTEEEIEFYI QQFKKTGFRG PLNWYRNTER NWKWSCKGLG RKILVPALMV TAEKDIVLRP EMSKNMEKWI PFLKRGHIED CGHWTQIEKP TEVNQILIKW LQTEVQNPSV TSKI // ID HYES_RAT STANDARD; PRT; 554 AA. AC P80299; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Soluble epoxide hydrolase (SEH) (EC 3.3.2.3) (Epoxide hydratase) DE (Cytosolic epoxide hydrolase) (CEH). GN EPHX2. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=93352557; PubMed=8349641; RA Knehr M., Thomas H., Arand M., Gebel T., Zeller H.-D., Oesch F.; RT "Isolation and characterization of a cDNA encoding rat liver RT cytosolic epoxide hydrolase and its functional expression in RT Escherichia coli."; RL J. Biol. Chem. 268:17623-17627(1993). RN [2] RP SEQUENCE OF 450-554 FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=92077134; PubMed=1743286; RA Arand M., Knehr M., Thomas H., Zeller H.-D., Oesch F.; RT "An impaired peroxisomal targeting sequence leading to an unusual RT bicompartmental distribution of cytosolic epoxide hydrolase."; RL FEBS Lett. 294:19-22(1991). CC -!- FUNCTION: THIS ENZYME ACTS ON EPOXIDES (ALKENE OXIDES, OXIRANES) CC AND ARENE OXIDES. PLAYS A ROLE IN XENOBIOTIC METABOLISM CC BY DEGRADING POTENTIAL TOXIC EPOXIDES. ALSO DETERMINES STEADY- CC STATE LEVELS OF PHYSIOLOGICAL MEDIATORS. CC -!- CATALYTIC ACTIVITY: AN EPOXIDE + H(2)O = A GLYCOL. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND PEROXISOMAL. CC -!- INDUCTION: BY COMPOUNDS THAT CAUSE PEROXISOME PROLIFERATION CC SUCH AS CLOFIBRATE, TIADENOL AND FENOFIBRATE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65083; CAA46211.1; -. DR EMBL; X60328; CAA42898.1; -. DR PIR; A47503; A47503. DR InterPro; IPR003089; AB_hydrolase. DR InterPro; IPR000073; Abhydrolase. DR InterPro; IPR000639; Epox_hydrlse. DR InterPro; IPR000379; Est_lip_thioest_actsite. DR InterPro; IPR001454; Hydrolase. DR Pfam; PF00561; abhydrolase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00412; EPOXHYDRLASE. DR PRINTS; PR00413; HADHALOGNASE. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Hydrolase; Peroxisome; Detoxification; KW Aromatic hydrocarbons catabolism. FT ACT_SITE 333 333 BY SIMILARITY. FT ACT_SITE 495 495 BY SIMILARITY. FT ACT_SITE 523 523 BY SIMILARITY. FT SITE 552 554 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 554 AA; 62340 MW; 145FDCA53F582138 CRC64; MALRVAAFDL DGVLALPSIA GVLRHTEEAL ALPRDFLLGA FQMKFPEGPT EQLMKGKITF SQWVPLMDES CRKSSKACGA SLPENFSISE IFSQAMAARS INRPMLQAAA ALKKKGFTTC IVTNNWLDDS DKRDILAQMM CELSQHFDFL IESCQVGMIK PEPQIYKFVL DTLKAKPNEV VFLDDFGSNL KPARDMGMVT ILVRDTASAL RELEKVTGTQ FPEAPLPVPC SPNDVSHGYV TVKPGIRLHF VEMGSGPAIC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP PEIEEYAMEL LCEEMVTFLN KLGIPQAVFI GHDWAGVLVW NMALFHPERV RAVASLNTPL MPPNPEVSPM EVIRSIPVFN YQLYFQEPGV AEAELEKNMS RTFKSFFRTS DDMGLLTVNK ATEMGGILVG TPEDPKVSKI TTEEEIEYYI QQFKKSGFRG PLNWYRNTER NWKWSCKALG RKILVPALMV TAEKDIVLRP EMSKNMENWI PFLKRGHIED CGHWTQIEKP AEVNQILIKW LKTEIQNPSV TSKI // ID IDI1_HUMAN STANDARD; PRT; 227 AA. AC Q13907; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) (IPP isomerase) DE (Isopentenyl pyrophosphate isomerase). GN IDI1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94292171; PubMed=8020941; RA Xuan J.W., Kowalski J., Chambers A.F., Denhardt D.T.; RT "A human promyelocyte mRNA transiently induced by TPA is homologous RT to yeast IPP isomerase."; RL Genomics 20:129-131(1994). RN [2] RP CHARACTERIZATION. RX MEDLINE=96400329; PubMed=8806705; RA Hahn F.M., Xuan J.W., Chambers A.F., Poulter C.D.; RT "Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase: RT overproduction, purification, and characterization."; RL Arch. Biochem. Biophys. 332:30-34(1996). CC -!- FUNCTION: CATALYZES THE 1,3-ALLYLIC REARRANGEMENT OF THE CC HOMOALLYLIC SUBSTRATE ISOPENTENYL (IPP) TO ITS HIGHLY CC ELECTROPHILIC ALLYLIC ISOMER, DIMETHYLALLYL DIPHOSPHATE (DMAPP). CC -!- CATALYTIC ACTIVITY: ISOPENTENYL DIPHOSPHATE = DIMETHYLALLYL CC DIPHOSPHATE. CC -!- COFACTOR: REQUIRES MAGNESIUM FOR ACTIVITY. CC -!- PATHWAY: ISOPRENOID BIOSYNTHETIC PATHWAY WHOSE END PRODUCTS CC INCLUDE DOLICHOLS, VITAMINS A, D, E, AND K, STEROID HORMONES, CC CAROTENOIDS BILE ACIDS AND CHOLESTEROL. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE IPP ISOMERASE TYPE 1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17025; CAA34890.1; ALT_INIT. DR MIM; 604055; -. DR InterPro; IPR002667; Isopentdiph_delta_isomrse. DR InterPro; IPR000086; NUDIX_hydrolase. DR Pfam; PF00293; mutT; 1. DR ProDom; PD004109; Isopentdiph_delta_isomrse; 1. KW Isomerase; Isoprene biosynthesis; Cholesterol biosynthesis; KW Sterol biosynthesis; Peroxisome; Magnesium. FT ACT_SITE 86 86 BY SIMILARITY. FT ACT_SITE 148 148 BY SIMILARITY. FT SITE 225 227 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 227 AA; 26319 MW; 1255ACC2C4D1E8D1 CRC64; MPEINTNHLD KQQVQLLAEM CILIDENDNK IGAETKKNCH LNENIEKGLL HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNTCCSHPL SNPAELEESD ALGVRRAAQR RLKAELGIPL EEVPPEEINY LTRIHYKAQS DGIWGEHEID YILLVRKNVT LNPDPNEIKS YCYVSKEELK ELLKKAASGE IKITPWFKII AATFLFKWWD NLNHLNQFVD HEKIYRM // ID IDI1_MESAU STANDARD; PRT; 227 AA. AC O35586; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) (IPP isomerase) DE (Isopentenyl pyrophosphate isomerase). GN IDI1. OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Cricetinae; OC Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97373600; PubMed=9228075; RA Paton V.G., Shackelford J.E., Krisans S.K.; RT "Cloning and subcellular localization of hamster and rat isopentenyl RT diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets RT the enzyme to peroxisomes."; RL J. Biol. Chem. 272:18945-18950(1997). CC -!- FUNCTION: CATALYZES THE 1,3-ALLYLIC REARRANGEMENT OF THE CC HOMOALLYLIC SUBSTRATE ISOPENTENYL (IPP) TO ITS HIGHLY CC ELECTROPHILIC ALLYLIC ISOMER, DIMETHYLALLYL DIPHOSPHATE (DMAPP). CC -!- CATALYTIC ACTIVITY: ISOPENTENYL DIPHOSPHATE = DIMETHYLALLYL CC DIPHOSPHATE. CC -!- COFACTOR: REQUIRES MAGNESIUM FOR ACTIVITY. CC -!- PATHWAY: ISOPRENOID BIOSYNTHETIC PATHWAY WHOSE END PRODUCTS CC INCLUDE DOLICHOLS, VITAMINS A, D, E, AND K, STEROID HORMONES, CC CAROTENOIDS BILE ACIDS AND CHOLESTEROL. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE IPP ISOMERASE TYPE 1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF003836; AAC53283.1; -. DR InterPro; IPR002667; Isopentdiph_delta_isomrse. DR InterPro; IPR000086; NUDIX_hydrolase. DR Pfam; PF00293; mutT; 1. DR ProDom; PD004109; Isopentdiph_delta_isomrse; 1. KW Isomerase; Isoprene biosynthesis; Cholesterol biosynthesis; KW Sterol biosynthesis; Peroxisome; Magnesium. FT ACT_SITE 86 86 BY SIMILARITY. FT ACT_SITE 148 148 BY SIMILARITY. FT SITE 225 227 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 227 AA; 26317 MW; F500A6586385E803 CRC64; MPEINTSHLD EQQVQLLAEM CILIDENDNK IGADTKKNCH LNENIDKGLL HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNSCCSHPL SNPGELEEND AIGVKRAAQR RLKAELGIPL EEVDPNEMHY LTRIYYKAQS DGIWGEHEID YILFLKKNVT LNPDPNEIKS YCYVSKEELK ELVKKAASGE VKLTPWFKII VDTFLFKWWD NLNHLSQFVD HEKIHRM // ID IDI1_MOUSE STANDARD; PRT; 227 AA. AC P58044; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) (IPP isomerase) DE (Isopentenyl pyrophosphate isomerase). GN IDI1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DH10B; TISSUE=Breast tumor; RA Strausberg R.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE 1,3-ALLYLIC REARRANGEMENT OF THE CC HOMOALLYLIC SUBSTRATE ISOPENTENYL (IPP) TO ITS HIGHLY CC ELECTROPHILIC ALLYLIC ISOMER, DIMETHYLALLYL DIPHOSPHATE (DMAPP) CC (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ISOPENTENYL DIPHOSPHATE = DIMETHYLALLYL CC DIPHOSPHATE. CC -!- COFACTOR: REQUIRES MAGNESIUM FOR ACTIVITY (BY SIMILARITY). CC -!- PATHWAY: ISOPRENOID BIOSYNTHETIC PATHWAY WHOSE END PRODUCTS CC INCLUDE DOLICHOLS, VITAMINS A, D, E, AND K, STEROID HORMONES, CC CAROTENOIDS BILE ACIDS AND CHOLESTEROL. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE IPP ISOMERASE TYPE 1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; BC004801; AAH04801.1; -. DR ProDom; PD004109; Isopentdiph_delta_isomrse; 1. KW Isomerase; Isoprene biosynthesis; Cholesterol biosynthesis; KW Sterol biosynthesis; Peroxisome; Magnesium. FT ACT_SITE 86 86 BY SIMILARITY. FT ACT_SITE 148 148 BY SIMILARITY. FT SITE 225 227 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 227 AA; 26289 MW; 2B0D1176B9E328D4 CRC64; MPEINTSHLD EKQVQLLAEM CILIDENDNK IGADTKKNCH LNENIDKGLL HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNSCCSHPL SNPGELEENN AIGVKRAAKR RLKAELGIPL EEVDLNEMDY LTRIYYKAQS DGIWGEHEVD YILFLRKNVT LNPDPNEIKS YCYVSKEEVR EILKKAASGE IKLTPWFKII ADTFLFKWWD NLNHLSPFVD HEKIHRL // ID IDI1_RAT STANDARD; PRT; 227 AA. AC O35760; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isopentenyl-diphosphate delta-isomerase (EC 5.3.3.2) (IPP isomerase) DE (Isopentenyl pyrophosphate isomerase). GN IDI1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=97373600; PubMed=9228075; RA Paton V.G., Shackelford J.E., Krisans S.K.; RT "Cloning and subcellular localization of hamster and rat isopentenyl RT diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif targets RT the enzyme to peroxisomes."; RL J. Biol. Chem. 272:18945-18950(1997). CC -!- FUNCTION: CATALYZES THE 1,3-ALLYLIC REARRANGEMENT OF THE CC HOMOALLYLIC SUBSTRATE ISOPENTENYL (IPP) TO ITS HIGHLY CC ELECTROPHILIC ALLYLIC ISOMER, DIMETHYLALLYL DIPHOSPHATE (DMAPP). CC -!- CATALYTIC ACTIVITY: ISOPENTENYL DIPHOSPHATE = DIMETHYLALLYL CC DIPHOSPHATE. CC -!- COFACTOR: REQUIRES MAGNESIUM FOR ACTIVITY. CC -!- PATHWAY: ISOPRENOID BIOSYNTHETIC PATHWAY WHOSE END PRODUCTS CC INCLUDE DOLICHOLS, VITAMINS A, D, E, AND K, STEROID HORMONES, CC CAROTENOIDS BILE ACIDS AND CHOLESTEROL. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE IPP ISOMERASE TYPE 1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF003835; AAC53282.1; -. DR InterPro; IPR002667; Isopentdiph_delta_isomrse. DR InterPro; IPR000086; NUDIX_hydrolase. DR Pfam; PF00293; mutT; 1. DR ProDom; PD004109; Isopentdiph_delta_isomrse; 1. KW Isomerase; Isoprene biosynthesis; Cholesterol biosynthesis; KW Sterol biosynthesis; Peroxisome; Magnesium. FT ACT_SITE 86 86 BY SIMILARITY. FT ACT_SITE 148 148 BY SIMILARITY. FT SITE 225 227 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 227 AA; 26402 MW; 089434FAE83DC39B CRC64; MPEINASNLD EKQVQLLAEM CILIDENDNK IGADTKKNCH LNENIDKGLI HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNSCCSHPL NNPGELEEND AMGVKRAAQK RLKAELGIPL EEVDLNEMNY LTRIYYKAQS DGIWGEHEID YILFLRKNVT LNPDPNEIKS YCYVSKEELK EILKKEARGE IKFTPWFKII ADAFLFKWWD NLNHLSPFVD HEKIHRM // ID LUCI_LUCCR STANDARD; PRT; 548 AA. AC P13129; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Luciferin 4-monooxygenase (EC 1.13.12.7) (Luciferase). OS Luciola cruciata (Japanese firefly) (Genji firefly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Elateriformia; Cantharoidea; Lampyridae; Luciola. OX NCBI_TaxID=7051; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89326143; PubMed=2473944; RA Masuda T., Tatsumi H., Nakano E.; RT "Cloning and sequence analysis of cDNA for luciferase of a Japanese RT firefly, Luciola cruciata."; RL Gene 77:265-270(1989). CC -!- FUNCTION: PRODUCES GREEN LIGHT WITH A WAVELENGTH OF 544 NM. CC -!- CATALYTIC ACTIVITY: LUCIFERIN + O(2) + ATP = OXIDIZED LUCIFERIN + CC CO(2) + H(2)O + AMP + PYROPHOSPHATE + LIGHT. CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ATP-DEPENDENT AMP-BINDING ENZYME CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26194; AAA29135.1; -. DR PIR; JS0181; JS0181. DR HSSP; P08659; 1LCI. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00455; AMP_BINDING; 1. KW Oxidoreductase; Monooxygenase; Photoprotein; Luminescence; Magnesium; KW Peroxisome. FT SITE 546 548 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 548 AA; 60017 MW; 2052D6189E79109F CRC64; MENMENDENI VVGPKPFYPI EEGSAGTQLR KYMERYAKLG AIAFTNAVTG VDYSYAEYLE KSCCLGKALQ NYGLVVDGRI ALCSENCEEF FIPVIAGLFI GVGVAPTNEI YTLRELVHSL GISKPTIVFS SKKGLDKVIT VQKTVTTIKT IVILDSKVDY RGYQCLDTFI KRNTPPGFQA SSFKTVEVDR KEQVALIMNS SGSTGLPKGV QLTHENTVTR FSHARDPIYG NQVSPGTAVL TVVPFHHGFG MFTTLGYLIC GFRVVMLTKF DEETFLKTLQ DYKCTSVILV PTLFAILNKS ELLNKYDLSN LVEIASGGAP LSKEVGEAVA RRFNLPGVRQ GYGLTETTSA IIITPEGDDK PGASGKVVPL FKAKVIDLDT KKSLGPNRRG EVCVKGPMLM KGYVNNPEAT KELIDEEGWL HTGDIGYYDE EKHFFIVDRL KSLIKYKGYQ VPPAELESVL LQHPSIFDAG VAGVPDPVAG ELPGAVVVLE SGKNMTEKEV MDYVASQVSN AKRLRGGVRF VDEVPKGLTG KIDGRAIREI LKKPVAKM // ID LUCI_LUCLA STANDARD; PRT; 548 AA. AC Q01158; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Luciferin 4-monooxygenase (EC 1.13.12.7) (Luciferase). OS Luciola lateralis (Firefly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Elateriformia; Cantharoidea; Lampyridae; Luciola. OX NCBI_TaxID=7052; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92305054; PubMed=1610896; RA Tatsumi H., Kajiyama N., Nakano E.; RT "Molecular cloning and expression in Escherichia coli of a cDNA clone RT encoding luciferase of a firefly, Luciola lateralis."; RL Biochim. Biophys. Acta 1131:161-165(1992). CC -!- FUNCTION: PRODUCES GREEN LIGHT. CC -!- CATALYTIC ACTIVITY: LUCIFERIN + O(2) + ATP = OXIDIZED LUCIFERIN + CC CO(2) + H(2)O + AMP + PYROPHOSPHATE + LIGHT. CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ATP-DEPENDENT AMP-BINDING ENZYME CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66919; CAA47358.1; -. DR PIR; S23437; S23437. DR HSSP; P08659; 1LCI. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00455; AMP_BINDING; 1. KW Oxidoreductase; Monooxygenase; Photoprotein; Luminescence; Magnesium; KW Peroxisome. FT SITE 546 548 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 548 AA; 60125 MW; AC62F9320BB6D4A6 CRC64; MENMENDENI VYGPEPFYPI EEGSAGAQLR KYMDRYAKLG AIAFTNALTG VDYTYAEYLE KSCCLGEALK NYGLVVDGRI ALCSENCEEF FIPVLAGLFI GVGVAPTNEI YTLRELVHSL GISKPTIVFS SKKGLDKVIT VQKTVTAIKT IVILDSKVDY RGYQSMDNFI KKNTPQGFKG SSFKTVEVNR KEQVALIMNS SGSTGLPKGV QLTHENAVTR FSHARDPIYG NQVSPGTAIL TVVPFHHGFG MFTTLGYLTC GFRIVMLTKF DEETFLKTLQ DYKCSSVILV PTLFAILNRS ELLDKYDLSN LVEIASGGAP LSKEIGEAVA RRFNLPGVRQ GYGLTETTSA IIITPEGDDK PGASGKVVPL FKAKVIDLDT KKTLGPNRRG EVCVKGPMLM KGYVDNPEAT REIIDEEGWL HTGDIGYYDE EKHFFIVDRL KSLIKYKGYQ VPPAELESVL LQHPNIFDAG VAGVPDPIAG ELPGAVVVLE KGKSMTEKEV MDYVASQVSN AKRLRGGVRF VDEVPKGLTG KIDGKAIREI LKKPVAKM // ID LUCI_PHOPY STANDARD; PRT; 550 AA. AC P08659; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Luciferin 4-monooxygenase (EC 1.13.12.7) (Luciferase). OS Photinus pyralis (North American firefly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Elateriformia; Cantharoidea; Lampyridae; Photinus. OX NCBI_TaxID=7054; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87144243; PubMed=3821727; RA de Wet J.R., Wood K.V., Deluca M., Helinski D.R., Subramani S.; RT "Firefly luciferase gene: structure and expression in mammalian RT cells."; RL Mol. Cell. Biol. 7:725-737(1987). RN [2] RP SUBCELLULAR LOCATION. RX MEDLINE=87204117; PubMed=3554235; RA Keller G.-A., Gould S., de Luca M., Subramani S.; RT "Firefly luciferase is targeted to peroxisomes in mammalian cells."; RL Proc. Natl. Acad. Sci. U.S.A. 84:3264-3268(1987). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=96398615; PubMed=8805533; RA Conti E., Franks N.P., Brick P.; RT "Crystal structure of firefly luciferase throws light on a RT superfamily of adenylate-forming enzymes."; RL Structure 4:287-298(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=99007339; PubMed=9788915; RA Franks N.P., Jenkins A., Conti E., Lieb W.R., Brick P.; RT "Structural basis for the inhibition of firefly luciferase by a RT general anesthetic."; RL Biophys. J. 75:2205-2211(1998). CC -!- FUNCTION: PRODUCES GREEN LIGHT WITH A WAVELENGTH OF 562 NM. CC -!- CATALYTIC ACTIVITY: LUCIFERIN + O(2) + ATP = OXIDIZED LUCIFERIN + CC CO(2) + H(2)O + AMP + PYROPHOSPHATE + LIGHT. CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE ATP-DEPENDENT AMP-BINDING ENZYME CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15077; AAA29795.1; -. DR EMBL; X84848; CAA59283.1; -. DR EMBL; U03687; AAA03561.1; -. DR EMBL; U89934; AAB64396.1; -. DR EMBL; U89935; AAB64399.1; -. DR PIR; A26772; A26772. DR PDB; 1LCI; 26-MAR-97. DR PDB; 1BA3; 11-NOV-98. DR InterPro; IPR000873; AMP-bind. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00455; AMP_BINDING; 1. KW Oxidoreductase; Monooxygenase; Photoprotein; Luminescence; Magnesium; KW Peroxisome; 3D-structure. FT SITE 548 550 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 550 AA; 60745 MW; E380FCE9D56ACCDE CRC64; MEDAKNIKKG PAPFYPLEDG TAGEQLHKAM KRYALVPGTI AFTDAHIEVN ITYAEYFEMS VRLAEAMKRY GLNTNHRIVV CSENSLQFFM PVLGALFIGV AVAPANDIYN ERELLNSMNI SQPTVVFVSK KGLQKILNVQ KKLPIIQKII IMDSKTDYQG FQSMYTFVTS HLPPGFNEYD FVPESFDRDK TIALIMNSSG STGLPKGVAL PHRTACVRFS HARDPIFGNQ IIPDTAILSV VPFHHGFGMF TTLGYLICGF RVVLMYRFEE ELFLRSLQDY KIQSALLVPT LFSFFAKSTL IDKYDLSNLH EIASGGAPLS KEVGEAVAKR FHLPGIRQGY GLTETTSAIL ITPEGDDKPG AVGKVVPFFE AKVVDLDTGK TLGVNQRGEL CVRGPMIMSG YVNNPEATNA LIDKDGWLHS GDIAYWDEDE HFFIVDRLKS LIKYKGYQVA PAELESILLQ HPNIFDAGVA GLPDDDAGEL PAAVVVLEHG KTMTEKEIVD YVASQVTTAK KLRGGVVFVD EVPKGLTGKL DARKIREILI KAKKGGKSKL // ID MDHP_YEAST STANDARD; PRT; 342 AA. AC P32419; Q12689; DT 01-OCT-1993 (Rel. 27, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate dehydrogenase, peroxisomal (EC 1.1.1.37). GN MDH3 OR YDL078C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-15; 22-35 AND 152-166. RX MEDLINE=93077569; PubMed=1447211; RA Steffan J.S., McAlister-Henn L.; RT "Isolation and characterization of the yeast gene encoding the MDH3 RT isozyme of malate dehydrogenase."; RL J. Biol. Chem. 267:24708-24715(1992). RN [2] RP SEQUENCE FROM N.A. RA Wambutt R., Wedler H., Wedler E., Scharfe M.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-MALATE + NAD(+) = OXALOACETATE + NADH. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- MISCELLANEOUS: YEAST CONTAINS AT LEAST 3 MALATE DEHYDROGENASE CC ISOENZYMES: A MITOCHONDRIAL (MDH1), A CYTOPLASMIC (MDH2) AND A CC PEROXISOMAL (MDH3). CC -!- SIMILARITY: BELONGS TO THE LDH FAMILY. MDH SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M98763; AAA34767.1; -. DR EMBL; Z74126; CAA98644.1; -. DR PIR; S31255; DEBYMP. DR HSSP; P00346; 1MLD. DR SGD; S0002236; MDH3. DR InterPro; IPR001252; MDH_actsite. DR InterPro; IPR001236; ldh. DR Pfam; PF00056; ldh; 1. DR PROSITE; PS00068; MDH; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Tricarboxylic acid cycle; NAD; Glyoxylate bypass; KW Peroxisome. FT INIT_MET 0 0 FT ACT_SITE 148 148 PROTON-RELAY (BY SIMILARITY). FT BINDING 151 151 SUBSTRATE CARBOXYL GROUP (BY SIMILARITY). FT ACT_SITE 186 186 PROTON-RELAY (BY SIMILARITY). FT SITE 340 342 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 239 239 A -> R (IN REF. 1). SQ SEQUENCE 342 AA; 37055 MW; 1230D9CA632E5C4A CRC64; VKVAILGASG GVGQPLSLLL KLSPYVSELA LYDIRAAEGI GKDLSHINTN SSCVGYDKDS IENTLSNAQV VLIPAGVPRK PGLTRDDLFK MNAGIVKSLV TAVGKFAPNA RILVISNPVN SLVPIAVETL KKMGKFKPGN VMGVTNLDLV RAETFLVDYL MLKNPKIGQE QDKTTMHRKV TVIGGHSGET IIPIITDKSL VFQLDKQYEH FIHRVQFGGD EIVKAKQGAG SATLSMAFAG AKFAEEVLRS FHNEKPETES LSAFVYLPGL KNGKKAQQLV GDNSIEYFSL PIVLRNGSVV SIDTSVLEKL SPREEQLVNT AVKELRKNIE KGKSFILDSS KL // ID MLF2_MALFU STANDARD; PRT; 177 AA. AC P56577; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Allergen Mal f 2 (MF1). OS Malassezia furfur (Pityriasis versicolor infection agent) OS (Pityrosporum orbiculare). OC Eukaryota; Fungi; Basidiomycota; Ustilaginomycetes; OC Exobasidiomycetidae; Malasseziales; Malassezia. OX NCBI_TaxID=55194; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TIMM2782; RX MEDLINE=98342073; PubMed=9675120; RA Yasueda H., Hashida-Okado T., Saito A., Uchida K., Kuroda M., RA Onishi Y., Takahashi K., Yamaguchi H., Takesako K., Akiyama K.; RT "Identification and cloning of two novel allergens from the RT lipophilic yeast, Malassezia furfur."; RL Biochem. Biophys. Res. Commun. 248:240-244(1998). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PEROXIREDOXIN 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB011804; BAA32435.1; -. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. KW Peroxisome; Allergen. FT SITE 175 177 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). SQ SEQUENCE 177 AA; 19193 MW; 1E1F907C68E51031 CRC64; MPGDPTATAK GNEIPDTLMG YIPWTPELDS GEVCGIPTTF KTRDEWKGKK VVIVSIPGAY TPICHQQHIP PLVKRVDELK AKGVDAVYVI ASNDPFVMAA WGNFNNAKDK VVFATDIDLA FSKALGATID LSAKHFGERT ARYALIIDDN KIVDFASDEG DTGKLQNASI DTILTKV // ID MLF3_MALFU STANDARD; PRT; 166 AA. AC P56578; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Allergen Mal f 3 (MF2) (Fragment). OS Malassezia furfur (Pityriasis versicolor infection agent) OS (Pityrosporum orbiculare). OC Eukaryota; Fungi; Basidiomycota; Ustilaginomycetes; OC Exobasidiomycetidae; Malasseziales; Malassezia. OX NCBI_TaxID=55194; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TIMM2782; RX MEDLINE=98342073; PubMed=9675120; RA Yasueda H., Hashida-Okado T., Saito A., Uchida K., Kuroda M., RA Onishi Y., Takahashi K., Yamaguchi H., Takesako K., Akiyama K.; RT "Identification and cloning of two novel allergens from the RT lipophilic yeast, Malassezia furfur."; RL Biochem. Biophys. Res. Commun. 248:240-244(1998). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE PEROXIREDOXIN 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB011805; BAA32436.1; -. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. KW Peroxisome; Allergen. FT NON_TER 1 1 FT SITE 164 166 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). SQ SEQUENCE 166 AA; 18145 MW; 22AF20B892645B97 CRC64; EIGSTIPNAT FAYVPYSPEL EDHKVCGMPT SFQSHERWKG KKVVIVAVPG AFTPTCTANH VPPYVEKIQE LKSKGVDEVV VISANDPFVL SAWGITEHAK DNLTFAQDVN CEFSKHFNAT LDLSSKGMGL RTARYALIAN DLKVEYFGID EGEPKQSSAA TVLSKL // ID OCTC_BOVIN STANDARD; PRT; 612 AA. AC O19094; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal carnitine octanoyltransferase (EC 2.3.1.-) (COT). GN COT. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A., AND MUTAGENESIS. RC TISSUE=Liver; RX MEDLINE=97433288; PubMed=9288928; RA Cronin C.N.; RT "cDNA cloning, recombinant expression, and site-directed mutagenesis RT of bovine liver carnitine octanoyltransferase -- Arg505 binds the RT carboxylate group of carnitine."; RL Eur. J. Biochem. 247:1029-1037(1997). CC -!- FUNCTION: BETA-OXIDATION OF FATTY ACIDS. THE HIGHEST ACTIVITY CC CONCERN THE C6 TO C10 CHAIN LENGTH SUBSTRATE. CC -!- PATHWAY: FATTY ACID BETA-OXIDATION. CC -!- SUBUNIT: MONOMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U65745; AAC48758.1; -. DR InterPro; IPR000542; Carn_acyltransf. DR InterPro; IPR000865; Microbodies_C. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; FALSE_NEG. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome. FT ACT_SITE 327 327 POTENTIAL. FT BINDING 505 505 INVOLVED IN SUBSTRATE (CARNITINE) FT BINDING. FT DOMAIN 534 537 POLY-GLY. FT SITE 610 612 MICROBODY TARGETING SIGNAL (POTENTIAL). FT MUTAGEN 505 505 R->N:INCREASE OF KM TOWARDS CARNITINE. SQ SEQUENCE 612 AA; 70263 MW; 2D5D91A54CF8E2BA CRC64; MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANEEEYKN TEAIVWKFQN GIGEKLQQKL LQRAKGRRNW LEEWWLNVAY LDVRIPSQLN VNFGGPASHI EHYWPPKEGT QLERGSISLW HNLNYWQLLR KEKLAVEKVG NTPLDMNQFR MLFSTCKIPG ITRDSIINYF RTESEGHSPS HLAVLCRGRV FVFDVMHEGY LMTAPEIQRQ LTYIQKKCHS EPDGPGVAAL TTEERTRWAK AREYLISLNP ENLTILEKIQ SSLLVFCLDD DSPHVTPEDY SQVSAKILNG DPTVRWGDKS YNLIAFSNGV FGSNCDHAPF DAMVLVKVCY YVDENILENE GRWKGSEKVR DIPVPEELVF TVDEKVLNDI NQAKAQYFKQ VSDLQLVVYA FTSFGKKLTK EKQLHPDTFI QLALQLAYYR LHGRPGCCYE TAMTRLFYHG RTETVRPCTV EAVNWCQSMQ NPSTSLLERK HMMLEAFAKH NKMMKDCSTG KGFDRHLLGL SLIAKEEGLP VPELFTDPLF SRSGGGGNFV LSTSLVGYLR VQGVMVPMVH NGYGFFYHIR DDRFVVSCSA WKSCPETDAE KLVQQVFHAF CDMMQLMEMP HL // ID OCTC_HUMAN STANDARD; PRT; 612 AA. AC Q9UKG9; Q9Y6I2; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal carnitine octanoyltransferase (EC 2.3.1.-) (COT). GN COT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC TISSUE=Skin; RX MEDLINE=99417547; PubMed=10486279; RA Ferdinandusse S., Mulders J., Ijlst L., Denis S., Dacremont G., RA Waterham H.R., Wanders R.J.A.; RT "Molecular cloning and expression of human carnitine RT octanoyltransferase: evidence for its role in the peroxisomal beta- RT oxidation of branched-chain fatty acids."; RL Biochem. Biophys. Res. Commun. 263:213-218(1999). RN [2] RP SEQUENCE FROM N.A. RA Kim D.G., Hlubb C.W., Yun J., Mihalik S.J.; RT "Cloning of the human gene for carnitine octanoyltransferase."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: BETA-OXIDATION OF FATTY ACIDS. THE HIGHEST ACTIVITY CC CONCERN THE C6 TO C10 CHAIN LENGTH SUBSTRATE. CONVERTS THE END CC PRODUCT OF PRISTANIC ACID BETA OXIDATION, 4,8-DIMETHYLNONANOYL- CC COA, TO ITS CORRESPONDING CARNITINE ESTER. CC -!- PATHWAY: FATTY ACID BETA-OXIDATION. CC -!- SUBUNIT: MONOMER (PROBABLE). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF168793; AAF03234.1; -. DR EMBL; AF073770; AAD41654.1; -. DR InterPro; IPR000542; Carn_acyltransf. DR InterPro; IPR000865; Microbodies_C. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; FALSE_NEG. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome. FT ACT_SITE 327 327 POTENTIAL. FT BINDING 505 505 INVOLVED IN SUBSTRATE (CARNITINE) FT BINDING (BY SIMILARITY). FT DOMAIN 534 537 POLY-GLY. FT SITE 610 612 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 144 144 L -> V (IN REF. 2). FT CONFLICT 168 168 V -> G (IN REF. 2). SQ SEQUENCE 612 AA; 70192 MW; 39C23B769A54A2F3 CRC64; MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANQEEYKK TEEIVQKFQS GIGEKLHQKL LERAKGKRNW LEEWWLNVAY LDVRIPSQLN VNFAGPAAHF EHYWPPKEGT QLERGSITLW HNLNYWQLLR KEKLPVHKVG NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF RTESEGRSPN HIVVLCRGRA FVFDVIHEGC LVTPPELLRQ LTYIHKKCHS EPDGPGIAAL TSEERTRWAK AREYLIGLDP ENLALLEKIQ SSLLVYSMED SSPHVTPEDY SEIIAAILIG DPTVRWGDKS YNLISFSNGV FGCNCDHAPF DAMIMVNISY YVDEKIFQNE GRWKGSEKVR DIPLPEELIF IVDEKVLNDI NQAKAQYLRE ASDLQIAAYA FTSFGKKLTK NKMLHPDTFI QLALQLAYYR LHGHPGCCYE TAMTRHFYHG RTETMRSCTV EAVRWCQSMQ DPSVNLRERQ QKMLQAFAKH NKMMKDCSAG KGFDRHLLGL LLIAKEEGLP VPELFTDPLF SKSGGGGNFV LSTSLVGYLR VQGVVVPMVH NGYGFFYHIR DDRFVVACSA WKSCPETDAE KLVQLTFCAF HDMIQLMNST HL // ID OCTC_RAT STANDARD; PRT; 612 AA. AC P11466; P48033; DT 01-OCT-1989 (Rel. 12, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal carnitine octanoyltransferase (EC 2.3.1.-) (COT). GN COT. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=96085126; PubMed=7495866; RA Choi S.J., Oh D.H., Song C.S., Roy A.K., Chatterjee B.; RT "Molecular cloning and sequence analysis of the rat liver carnitine RT octanoyltransferase cDNA, its natural gene and the gene promoter."; RL Biochim. Biophys. Acta 1264:215-222(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=89166509; PubMed=3233218; RA Chatterjee B., Song C.S., Kim J.-M., Roy A.K.; RT "Cloning, sequencing, and regulation of rat liver carnitine RT octanoyltransferase: transcriptional stimulation of the enzyme during RT peroxisome proliferation."; RL Biochemistry 27:9000-9006(1988). CC -!- FUNCTION: BETA-OXIDATION OF FATTY ACIDS. THE HIGHEST ACTIVITY CC CONCERN THE C6 TO C10 CHAIN LENGTH SUBSTRATE. CC -!- PATHWAY: FATTY ACID BETA-OXIDATION. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- TISSUE SPECIFICITY: LIVER. CC -!- SIMILARITY: BELONGS TO THE CARNITINE/CHOLINE ACETYLTRANSFERASE CC FAMILY. CC -!- CAUTION: REF.1 SEQUENCE WAS INCORRECT, STARTING WITH POSITION 548. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U26033; AAC52317.1; -. DR EMBL; J02844; AAA40948.1; ALT_SEQ. DR PIR; A31948; A31948. DR InterPro; IPR000542; Carn_acyltransf. DR Pfam; PF00755; Carn_acyltransf; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. KW Transferase; Acyltransferase; Fatty acid metabolism; Transport; KW Peroxisome. FT ACT_SITE 327 327 POTENTIAL. FT BINDING 505 505 INVOLVED IN SUBSTRATE (CARNITINE) BINDING FT (BY SIMILARITY). FT DOMAIN 534 537 POLY-GLY. FT SITE 610 612 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 334 334 L -> F (IN REF. 2). FT CONFLICT 463 464 VR -> RQ (IN REF. 2). SQ SEQUENCE 612 AA; 70302 MW; 41B2F3474C8838D1 CRC64; MENQLAKSIE ERTFQYQDSL PPLPVPSLEE SLKKYLESVK PFANEDEYKK TEEIVQKFQD GVGKTLHQKL LERAKGKRNW LEEWWLNVAY LDVRIPSQLN VNFVGPSPHF EHYWPAREGT QLERGSILLW HNLNYWQLLR REKLPVHKSG NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF KTESEGHCPT HIAVLCRGRA FVFDVLHDGC LITPPELLRQ LTYIYQKCWN EPVGPSIAAL TSEERTRWAK AREYLIGLDP ENLTLLEKIQ SSLFVYSIED TSPHATPENF SQVFEMLLGG DPAVRWGDKS YNLISFANGI FGCSCDHAPY DAMLMVNIAH YVDEKLLETE GRWKGSEKVR DIPLPEELAF TVDEKILNDV YQAKAQHLKA ASDLQIAAST FTSFGKKLTK KEALHPDTFI QLALQLAYYR LHGRPGCCYE TAMTRYFYHG RTETVRSCTV EAVRWCQSMQ DPSASLLERQ QKMLDAFAKH NKMMRDCSHG KGFDRHLLGL LLIAKEEGLP VPELFEDPLF SRSGGGGNFV LSTSLVGYLR IQGVVVPMVH NGYGFFYHIR DDRFVVTCSS WRSCLETDAE KLVEMIFHAF HDMIHLMNTA HL // ID OXDA_FUSSO STANDARD; PRT; 361 AA. AC P24552; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). OS Fusarium solani (subsp. pisi) (Nectria haematococca). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreales; mitosporic Hypocreales; Fusarium. OX NCBI_TaxID=109625; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=M-0718 / FERM P-2688; RX MEDLINE=91210207; PubMed=1982443; RA Isogai T., Ono H., Ishitani Y., Kojo H., Ueda Y., Kohsaka M.; RT "Structure and expression of cDNA for D-amino acid oxidase active RT against cephalosporin C from Fusarium solani."; RL J. Biochem. 108:1063-1069(1990). CC -!- FUNCTION: THIS ENZYME CAN EFFECTIVELY CONVERT CEPHALOSPORIN C CC INTO 7-BETA-(5-CARBOXY-5-OXOPENTANAMIDO)-CEPHALOSPORINIC ACID. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D00809; BAA00692.1; -. DR PIR; JX0152; JX0152. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00677; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 5 19 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 242 242 BY SIMILARITY. FT ACT_SITE 327 327 BY SIMILARITY. FT SITE 359 361 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 361 AA; 39696 MW; 148119480E2A67A5 CRC64; MSNTIVVVGA GVIGLTSALL LSKNKGNKIT VVAKHMPGDY DVEYASPFAG ANHSPMATEE SSEWERRTWY EFKRLVEEVP EAGVHFQKSR IQRRNVDTEK AQRSGFPDAL FSKEPWFKNM FEDFREQHPS EVIPGYDSGC EFTSVCINTA IYLPWLLGQC IKNGVIVKRA ILNDISEAKK LSHAGKTPNI IVNATGLGSY KLGGVEDKTM APARGQIVVV RNESSPMLLT SGVEDGGADV MYLMQRAAGG GTILGGTYDV GNWESQPDPN IANRIMQRIV EVRPEIANGK GVKGLSVIRH AVGMRPWRKD GVRIEEEKLD DETWIVHNYG HSGWGYQGSY GCAENVVQLV DKVGKAAKSK L // ID OXDA_HUMAN STANDARD; PRT; 347 AA. AC P14920; Q16758; DT 01-APR-1990 (Rel. 14, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). GN DAO OR DAMOX. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=89005666; PubMed=2901986; RA Momoi K., Fukui K., Watanabe F., Miyake Y.; RT "Molecular cloning and sequence analysis of cDNA encoding human RT kidney D-amino acid oxidase."; RL FEBS Lett. 238:180-184(1988). RN [2] RP REVISIONS. RA Momoi K.; RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 1-65 FROM N.A. RX MEDLINE=92406774; PubMed=1356107; RA Fukui K., Miyake Y.; RT "Molecular cloning and chromosomal localization of a human gene RT encoding D-amino-acid oxidase."; RL J. Biol. Chem. 267:18631-18638(1992). CC -!- FUNCTION: COULD ACT AS A DETOXIFYING AGENT WHICH REMOVES D-AMINO CC ACIDS ACCUMULATED DURING AGING. ACTS ON A VARIETY OF D-AMINO ACIDS CC WITH A PREFERENCE FOR THOSE HAVING SMALL HYDROPHOBIC SIDE CHAINS CC FOLLOWED BY THOSE BEARING POLAR, AROMATIC, AND BASIC GROUPS. DOES CC NOT ACT ON ACIDIC AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13227; CAA31614.1; -. DR EMBL; D11370; BAA20974.1; -. DR PIR; S01340; S01340. DR HSSP; P00371; 1DAO. DR MIM; 124050; -. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00677; DAO; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 3 17 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 228 228 BY SIMILARITY. FT ACT_SITE 307 307 BY SIMILARITY. FT SITE 345 347 MICROBODY TARGETING SIGNAL. FT CONFLICT 31 31 H -> D (IN REF. 3). SQ SEQUENCE 347 AA; 39411 MW; 3D59DA07E5A5DC68 CRC64; MRVVVIGAGV IGLSTALCIH ERYHSVLQPL HIKVYADRFT PLTTTDVAAG LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGEAT GFRPVRPQIR LEREQLRTGP SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL // ID OXDA_MOUSE STANDARD; PRT; 346 AA. AC P18894; Q64465; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). GN DAO OR DAO1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=90382679; PubMed=1976103; RA Tada M., Fukui K., Momoi K., Miyake Y.; RT "Cloning and expression of a cDNA encoding mouse kidney D-amino acid RT oxidase."; RL Gene 90:293-297(1990). RN [2] RP SEQUENCE FROM N.A. RA Sasaki M.; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP MUTAGENESIS OF GLY-182. RX MEDLINE=92385496; PubMed=1355365; RA Sasaki M., Konno R., Nishio M., Niwa A., Yasumura Y., Enami J.; RT "A single-base-pair substitution abolishes D-amino-acid oxidase RT activity in the mouse."; RL Biochim. Biophys. Acta 1139:315-318(1992). CC -!- FUNCTION: COULD ACT AS A DETOXIFYING AGENT WHICH REMOVES D-AMINO CC ACIDS ACCUMULATED DURING AGING. ACTS ON A VARIETY OF D-AMINO ACIDS CC WITH A PREFERENCE FOR THOSE HAVING SMALL HYDROPHOBIC SIDE CHAINS CC FOLLOWED BY THOSE BEARING POLAR, AROMATIC, AND BASIC GROUPS. DOES CC NOT ACT ON ACIDIC AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32299; AAA39367.1; -. DR EMBL; D10210; BAA01062.1; -. DR EMBL; D10211; BAA01063.1; -. DR PIR; JH0185; JH0185. DR HSSP; P00371; 1DAO. DR MGD; MGI:94859; Dao1. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00677; DAO; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 3 17 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 227 227 BY SIMILARITY. FT ACT_SITE 306 306 BY SIMILARITY. FT SITE 344 346 MICROBODY TARGETING SIGNAL. FT MUTAGEN 182 182 G->R: ABOLISHES ACTIVITY. FT CONFLICT 64 64 A -> V (IN REF. 1). FT CONFLICT 157 157 N -> K (IN REF. 1). FT CONFLICT 173 173 MISSING (IN REF. 1). SQ SEQUENCE 346 AA; 38714 MW; DFD18340675081C1 CRC64; MRVAVIGAGV IGLSTALCIH ERYHPTQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN PQEAEWSQQT FDYLLSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKNAV LGFRKLTPSE MDLFPDYGYG WFNTSLLLEG KSYLPWLTER LTERGVNLIH RKVESLEEVA RGGVDVIINC TGVWAGALQA DASLQPGRGQ IIQVEAPWIK HFILTHDPSL GIYNSPYIIP GSKTVTLGGI FQLGNWSGLN SVRDHNTIWK SCCKLEPTLK NARIVGELTG FRPVRPQVRL EREWLRFGSS SAEVIHNYGH GGYGLTIHWG CAMEAANLFG KILEEKKLSR LPPSHL // ID OXDA_PIG STANDARD; PRT; 347 AA. AC P00371; DT 21-JUL-1986 (Rel. 01, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). GN DAO. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=88000568; PubMed=2888479; RA Fukui K., Watanabe F., Shibata T., Miyake Y.; RT "Molecular cloning and sequence analysis of cDNAs encoding porcine RT kidney D-amino acid oxidase."; RL Biochemistry 26:3612-3618(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88137946; PubMed=2893757; RA Jacobs P., Brockly F., Massaer M., Loriau R., Guillaume J.P., RA Ciccarelli E., Heinderyckx M., Cravador A., Biemans R., van Elsen A., RA Herzog A., Bollen A.; RT "Porcine D-amino acid oxidase: determination of the mRNA nucleotide RT sequence by the characterization of genomic and cDNA clones."; RL Gene 59:55-61(1987). RN [3] RP SEQUENCE. RC TISSUE=Kidney; RX MEDLINE=89105024; PubMed=2905598; RA Nicholson B.H., Batra S.P.; RT "Structural interpretation of the binding of 9-azidoacridine to RT D-amino acid oxidase."; RL Biochem. J. 255:907-912(1988). RN [4] RP SEQUENCE. RC TISSUE=Kidney; RX MEDLINE=82239363; PubMed=6124543; RA Ronchi S., Minchiotti L., Galliano M., Curti B., Swenson R.P., RA Williams C.H. Jr., Massey V.; RT "The primary structure of D-amino acid oxidase from pig kidney. II. RT Isolation and sequence of overlap peptides and the complete RT sequence."; RL J. Biol. Chem. 257:8824-8834(1982). RN [5] RP PRELIMINARY STUDIES ON ACTIVE SITE. RX MEDLINE=82120157; PubMed=6120171; RA Swenson R.P., Williams C.H. Jr., Massey V.; RT "Chemical modification of D-amino acid oxidase. Amino acid sequence RT of the tryptic peptides containing tyrosine and lysine residues RT modified by fluorodinitrobenzene."; RL J. Biol. Chem. 257:1937-1944(1982). RN [6] RP PRELIMINARY STUDIES ON ACTIVE SITE. RX MEDLINE=83082913; PubMed=6129252; RA Swenson R.P., Williams C.H. Jr., Massey V.; RT "Identification of the histidine residue in D-amino acid oxidase that RT is covalently modified during inactivation by RT 5-dimethylaminonaphthalene-1-sulfonyl chloride."; RL J. Biol. Chem. 258:497-502(1983). RN [7] RP MUTAGENESIS OF Y-55/M-110/H-217 TO SHOW THEY ARE NOT IN ACTIVE SITE. RX MEDLINE=89005698; PubMed=2901989; RA Watanabe F., Fukui K., Momoi K., Miyake Y.; RT "Effect of site-specific mutagenesis of tyrosine-55, methionine-110 RT and histidine-217 in porcine kidney D-amino acid oxidase on its RT catalytic function."; RL FEBS Lett. 238:269-272(1988). RN [8] RP ACTIVE SITES TYR-228 AND HIS-307. RX MEDLINE=91201275; PubMed=1673125; RA Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M., RA Miyake Y.; RT "Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney RT D-amino acid oxidase: expression, purification, and RT characterization."; RL J. Biochem. 109:171-177(1991). RN [9] RP X-RAY CRYSTALLOGRAPHY. RX MEDLINE=97018220; PubMed=8864836; RA Mizutani H., Miyahara I., Hirotsu K., Nishima Y., Shiga K., RA Setoyama C., Miura R.; RT "Three-dimensional structure of porcine kidney D-amino acid oxidase RT at 3.0-A resolution."; RL J. Biochem. 120:14-17(1996). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=96353844; PubMed=8755502; RA Mattevi A., Vanoni M.A., Todone F., Rizzi M., Teplyakov A., Coda A., RA Bolognesi M., Curti B.; RT "Crystal structure of D-amino acid oxidase: a case of active site RT mirror-image convergent evolution with flavocytochrome b2."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7496-7501(1996). RN [11] RP X-RAY CRYSTALLOGRAPHY. RX MEDLINE=97297794; PubMed=9153426; RA Todone F., Vanoni M.A., Mozzarelli A., Bolognesi M., Coda A., RA Curti B., Mattevi A.; RT "Active site plasticity in D-amino acid oxidase: a crystallographic RT analysis."; RL Biochemistry 36:5853-5860(1997). CC -!- FUNCTION: COULD ACT AS A DETOXIFYING AGENT WHICH REMOVES D-AMINO CC ACIDS ACCUMULATED DURING AGING. ACTS ON A VARIETY OF D-AMINO ACIDS CC WITH A PREFERENCE FOR THOSE HAVING SMALL HYDROPHOBIC SIDE CHAINS CC FOLLOWED BY THOSE BEARING POLAR, AROMATIC, AND BASIC GROUPS. DOES CC NOT ACT ON ACIDIC AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -!- DATABASE: NAME=Worthington enzyme manual; CC WWW="http://www.worthington-biochem.com/manual/A/DAO.html". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16972; AAA30985.1; -. DR EMBL; M18447; AAA31025.1; -. DR EMBL; M18444; AAA31025.1; JOINED. DR EMBL; M18445; AAA31025.1; JOINED. DR EMBL; M18446; AAA31025.1; JOINED. DR EMBL; M18448; AAA31026.1; -. DR PIR; A00383; OXPGDA. DR PIR; A27209; A27209. DR PIR; A29598; A29598. DR PIR; A33798; A33798. DR PIR; S02656; S02656. DR PDB; 1KIF; 11-JUL-96. DR PDB; 1AA8; 21-APR-97. DR PDB; 1DAO; 23-JUL-97. DR PDB; 1DDO; 23-JUL-97. DR PDB; 1AN9; 12-NOV-97. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00677; DAO; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome; 3D-structure. FT NP_BIND 3 17 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 228 228 FT ACT_SITE 307 307 FT SITE 345 347 MICROBODY TARGETING SIGNAL. FT MUTAGEN 228 228 Y->F: REDUCES ACTIVITY. FT MUTAGEN 307 307 H->L: REDUCES ACTIVITY. SQ SEQUENCE 347 AA; 39336 MW; 0EC6577BDB2BF46C CRC64; MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DVKVYADRFT PFTTTDVAAG LWQPYTSEPS NPQEANWNQQ TFNYLLSHIG SPNAANMGLT PVSGYNLFRE AVPDPYWKDM VLGFRKLTPR ELDMFPDYRY GWFNTSLILE GRKYLQWLTE RLTERGVKFF LRKVESFEEV ARGGADVIIN CTGVWAGVLQ PDPLLQPGRG QIIKVDAPWL KNFIITHDLE RGIYNSPYII PGLQAVTLGG TFQVGNWNEI NNIQDHNTIW EGCCRLEPTL KDAKIVGEYT GFRPVRPQVR LEREQLRFGS SNTEVIHNYG HGGYGLTIHW GCALEVAKLF GKVLEERNLL TMPPSHL // ID OXDA_RABIT STANDARD; PRT; 347 AA. AC P22942; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). GN DAO. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Kidney; RX MEDLINE=91115787; PubMed=1980495; RA Momoi K., Fukui K., Tada M., Miyake Y.; RT "Gene expression of D-amino acid oxidase in rabbit kidney."; RL J. Biochem. 108:406-413(1990). CC -!- FUNCTION: COULD ACT AS A DETOXIFYING AGENT WHICH REMOVES D-AMINO CC ACIDS ACCUMULATED DURING AGING. ACTS ON A VARIETY OF D-AMINO ACIDS CC WITH A PREFERENCE FOR THOSE HAVING SMALL HYDROPHOBIC SIDE CHAINS CC FOLLOWED BY THOSE BEARING POLAR, AROMATIC, AND BASIC GROUPS. DOES CC NOT ACT ON ACIDIC AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D12494; BAA02058.1; -. DR PIR; JX0132; JX0132. DR HSSP; P00371; 1DAO. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00677; DAO; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 3 17 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 228 228 BY SIMILARITY. FT ACT_SITE 307 307 BY SIMILARITY. FT SITE 345 347 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 347 AA; 38590 MW; E22CFC0D944AFA61 CRC64; MRVVVIGAGV IGLSTALCIH ELYHSALQPL DMTIYADRFT PLTNTDVAAG LWQPYLSDPS NPQEADWSRQ TFNHLLSHIH SPSAEKMGLA LISGYNLFRK AVPDPSWKDT VLGFRKLTLR ELDMFPGYSY GWFNTSLILD GRSYLQWLTK RLTERGVKLF QRKVESFDEV AGGGVDVIVN CTGVWASALQ PDPLLQPGRG QIIKVDAPWV KHFIITHDPE SGIYKSPYII PGVHAVTLGG IFQMGNWSEG NSTDDHNTIW KGCCSLEPTL KDARIVGEWT GFRPVRPQIR LGREQLSAGP SKTEVIHNYG HGGYGLTIHW GCALEAAKLF GKILEEKKSS RMPPSHL // ID OXDA_RAT STANDARD; PRT; 346 AA. AC O35078; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). GN DAO. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; RX MEDLINE=98146267; PubMed=9473656; RA Konno R.; RT "Rat D-amino-acid oxidase cDNA: rat D-amino-acid oxidase as an RT intermediate form between mouse and other mammalian D-amino-acid RT oxidases."; RL Biochim. Biophys. Acta 1395:165-170(1998). CC -!- FUNCTION: COULD ACT AS A DETOXIFYING AGENT WHICH REMOVES D-AMINO CC ACIDS ACCUMULATED DURING AGING. ACTS ON A VARIETY OF D-AMINO ACIDS CC WITH A PREFERENCE FOR THOSE HAVING SMALL HYDROPHOBIC SIDE CHAINS CC FOLLOWED BY THOSE BEARING POLAR, AROMATIC, AND BASIC GROUPS. DOES CC NOT ACT ON ACIDIC AMINO ACIDS. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB003400; BAA22840.1; -. DR HSSP; P00371; 1DAO. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00677; DAO; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 3 17 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 227 227 BY SIMILARITY. FT ACT_SITE 306 306 BY SIMILARITY. FT SITE 344 346 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 346 AA; 38820 MW; 2C4697960137A4FE CRC64; MRVAVIGAGV IGLSTALCIH ERYHPAQPLH MKIYADRFTP FTTSDVAAGL WQPYLSDPSN PQEAEWNQQT FDHLQSCLHS PNAEKMGLAL ISGYNLFRDE VPDPFWKSTV LGFRKLTPSE LDMFPDYSYG WFNTSLLLEG KSYLSWLTER LTERGVKFIH RKVASFEEVV RGGVDVIINC TGVWAGALQA DASLQPGRGQ IIQVEAPWIK HFILTHDPSL GIYNSPYIIP GSKTVTLGGV FQLGNWSELN SVHDHNTIWK SCCQLEPTLK NARIMGELTG FRPVRPQVRL ERERLRFGSS SAEVIHNYGH GGYGLTIHWG CAMEAANLFG KILEEKNLSR MPPSHL // ID OXDA_RHOTO STANDARD; PRT; 368 AA. AC P80324; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE D-amino acid oxidase (EC 1.4.3.3) (DAMOX) (DAO) (DAAO). GN DAO1. OS Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis). OC Eukaryota; Fungi; Basidiomycota; Urediniomycetes; OC Microbotryomycetidae; Heterogastridiales; Sporidiobolaceae; OC Rhodosporidium. OX NCBI_TaxID=5286; RN [1] RP SEQUENCE. RA Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S.; RT "The primary structure of D-amino acid oxidase from Rhodotorula RT gracilis."; RL Biotechnol. Lett. 17:193-198(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 26217; RA Pilone M.S., Pollegioni L., Molla G., Campaner S., Martegani E.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 26217; RX MEDLINE=98240245; PubMed=9579082; RA Alonso J., Barredo J.L., Diez B., Salto F., Garcia J.L., Cortes E.; RT "D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium RT toruloides) ATCC 26217."; RL Microbiology 144:1095-1101(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CCRC 20306; RA Liaw G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP CHARACTERIZATION. RX MEDLINE=95382776; PubMed=7654197; RA Pollegioni L., Ceciliani F., Curti B., Ronchi S., Pilone M.S.; RT "Studies on the structural and functional aspects of Rhodotorula RT gracilis D-amino acid oxidase by limited trypsinolysis."; RL Biochem. J. 310:577-583(1995). CC -!- FUNCTION: THIS ENZYME CAN EFFECTIVELY CONVERT CEPHALOSPORIN C CC INTO 7-BETA-(5-CARBOXY-5-OXOPENTANAMIDO)-CEPHALOSPORINIC ACID. CC -!- CATALYTIC ACTIVITY: A D-AMINO ACID + H(2)O + O(2) = A 2-OXO-ACID + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60066; AAB51107.1; -. DR EMBL; Z71657; CAA96323.1; -. DR EMBL; AF003339; AAB93974.1; -. DR EMBL; AF003340; AAB93975.1; -. DR HSSP; P00371; 1DAO. DR InterPro; IPR000927; DAO. DR InterPro; IPR000205; NAD_binding. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00677; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT NP_BIND 7 21 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 223 223 BY SIMILARITY. FT ACT_SITE 329 329 BY SIMILARITY. FT SITE 366 368 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 368 AA; 40076 MW; 99940118BCFA886E CRC64; MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW AGANWTPFMT LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE DGLLGHWYKD ITPNYRPLPS SECPPGAIGV TYDTLSVHAP KYCQYLAREL QKLGATFERR TVTSLEQAFD GADLVVNATG LGAKSIAGID DQAAEPIRGQ TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV GDWDLSVNPE TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ LVDEAFQRYH GAARESKL // ID OXDD_BOVIN STANDARD; PRT; 341 AA. AC P31228; O02846; DT 01-JUL-1993 (Rel. 26, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE D-aspartate oxidase (EC 1.4.3.1) (DASOX) (DDO). GN DDO. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE OF 1-338. RC TISSUE=Kidney; RX MEDLINE=92291057; PubMed=1601857; RA Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S.; RT "The primary structure of the flavoprotein D-aspartate oxidase from RT beef kidney."; RL J. Biol. Chem. 267:11865-11871(1992). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Kidney cortex; RX MEDLINE=97220379; PubMed=9148742; RA Simonic T., Duga S., Negri A., Tedeschi G., Malcovati M., RA Tenchini M.L., Ronchi S.; RT "cDNA cloning and expression of the flavoprotein D-aspartate oxidase RT from bovine kidney cortex."; RL Biochem. J. 322:729-735(1997). CC -!- CATALYTIC ACTIVITY: D-ASPARTATE + H(2)O + O(2) = OXALOACETATE + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD OR 6-HYDROXYFLAVIN ADENINE DINUCLEOTIDE. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95310; CAA64622.1; -. DR PIR; A44132; A44132. DR HSSP; P00371; 1DAO. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00677; DAO; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome. FT MOD_RES 1 1 BLOCKED. FT NP_BIND 6 20 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 223 223 BY SIMILARITY. FT ACT_SITE 302 302 BY SIMILARITY. FT SITE 339 341 MICROBODY TARGETING SIGNAL (POTENTIAL). FT VARIANT 228 228 V -> I (IN SOME MOLECULES). FT CONFLICT 274 274 K -> R (IN REF. 1). FT CONFLICT 283 283 S -> G (IN REF. 1). SQ SEQUENCE 341 AA; 37659 MW; 355EF4EE42C53B49 CRC64; MDTVRIAVVG AGVMGLSTAV CISKMVPGCS ITVISDKFTP ETTSDVAAGM LIPPTYPDTP IQKQKQWFKE TFDHLFAIVN SAEAEDAGVI LVSGWQIFQS IPTEEVPYWA DVVLGFRKMT KDELKKFPQH VFGHAFTTLK CEGPAYLPWL QKRVKGNGGL ILTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR GQVLKVQAPW VKHFIRDSSG LTYIYPGVSN VTLGGTRQKG DWNLSPDAEI SKEILSRCCA LEPSLRGAYD LREKVGLRPT RPSVRLEKEL LAQDSRRLPV VHHYGHGSGG IAMHWGTALE ATRLVNECVQ VLRTPAPKSK L // ID OXDD_HUMAN STANDARD; PRT; 341 AA. AC Q99489; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE D-aspartate oxidase (EC 1.4.3.1) (DASOX) (DDO). GN DDO. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=97306065; PubMed=9163533; RA Setoyama C., Miura R.; RT "Structural and functional characterization of the human brain D- RT aspartate oxidase."; RL J. Biochem. 121:798-803(1997). CC -!- FUNCTION: SELECTIVELY CATALYZES THE OXIDATIVE DEAMINATION OF D- CC ASPARTATE AND ITS N-METHYLATED DERIVATIVE, N-METHYL D-ASPARTATE. CC -!- CATALYTIC ACTIVITY: D-ASPARTATE + H(2)O + O(2) = OXALOACETATE + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD OR 6-HYDROXYFLAVIN ADENINE DINUCLEOTIDE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; DDO-1 (SHOWN HERE) AND DDO-2; CC ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE DAMOX/DASOX FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D89858; BAA14031.1; -. DR HSSP; P00371; 1DAO. DR MIM; 124450; -. DR InterPro; IPR000927; DAO. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00677; DAO; 1. KW Oxidoreductase; Flavoprotein; FAD; Peroxisome; Alternative splicing. FT NP_BIND 6 20 FAD (ADP PART) (POTENTIAL). FT ACT_SITE 223 223 BY SIMILARITY. FT ACT_SITE 302 302 BY SIMILARITY. FT SITE 339 341 MICROBODY TARGETING SIGNAL (POTENTIAL). FT VARSPLIC 95 153 MISSING (IN ISOFORM DDO-2). SQ SEQUENCE 341 AA; 37535 MW; 8CAE7501FB7F215C CRC64; MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L // ID PECI_HUMAN STANDARD; PRT; 359 AA. AC O75521; Q9UN55; Q9NYH7; Q9NQH1; DT 15-JUL-1999 (Rel. 38, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8) (Dodecenoyl-CoA DE delta-isomerase) (D3,D2-enoyl-CoA isomerase) (DBI-related protein 1) DE (DRS-1) (Hepatocellular carcinoma-associated antigen 88). GN PECI OR DRS1 OR HCA88. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Pancreatic islets; RX MEDLINE=99284489; PubMed=10354522; RA Suk K., Kim Y.-H., Hwang D.-Y., Ihm S.-H., Yoo H.J., Lee M.-S.; RT "Molecular cloning and expression of a novel human cDNA related to the RT diazepam binding inhibitor."; RL Biochim. Biophys. Acta 1454:126-131(1999). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=99348312; PubMed=10419495; RA Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.; RT "Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA RT isomerase of mammalian peroxisomes."; RL J. Biol. Chem. 274:21797-21803(1999). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Hepatoma; RA Han K., Wang Y., Qu W., Pang X., Zhang H., Chen W.; RT "Cloning and characterization of novel genes related to human RT hepatocellular carcinoma."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RA Kay M.; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ABLE TO ISOMERIZE BOTH 3-CIS AND 3-TRANS DOUBLE BONDS CC INTO THE 2-TRANS FORM IN A RANGE OF ENOYL-COA SPECIES. CC -!- CATALYTIC ACTIVITY: 3-ENOYL-COA = 2-TRANS-ENOYL-COA. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL MATRIX. CC -!- TISSUE SPECIFICITY: ABUNDANT IN HEART, SKELETAL MUSCLE AND LIVER. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE ACBP FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE ENOYL-COA CC HYDRATASE/ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF069301; AAC19317.1; ALT_INIT. DR EMBL; AF153612; AAD34173.1; -. DR EMBL; AF244138; AAF66247.1; ALT_INIT. DR EMBL; AL033383; CAB94781.1; ALT_INIT. DR HSSP; P07107; 1ACA. DR InterPro; IPR000582; ACBP. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00887; ACBP; 1. DR Pfam; PF00378; ECH; 1. DR PRINTS; PR00689; ACOABINDINGP. DR ProDom; PD002965; ACBP; 1. DR PROSITE; PS00880; ACBP; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Isomerase; Peroxisome. FT DOMAIN 1 88 ACBP. FT DOMAIN 116 287 ECH-LIKE. FT SITE 357 359 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 160 160 Y -> C (IN REF. 1). FT CONFLICT 309 309 V -> A (IN REF. 2 AND 4). SQ SEQUENCE 359 AA; 39637 MW; B9EC799D628799F0 CRC64; MRASQKDFEN SMNQVKLLKK DPGNEVKLKL YALYKQATEG PCNMPKPGVF DLINKAKWDA WNALGSLPKE AARQNYVDLV SSLSPSLESS SQVEPGTDRK STGFETLVVT SEDGITKIMF NRPKKKNAIN TEMYHEIMRA LKAASKDDSI ITVLTGNGDY YSSGNDLTNF TDIPPGGVEE KAKNNAVLLR EFVGCFIDFP KPLIAVVNGP AVGISVTLLG LFDAVYASDR ATFHTPFSHL GQSPEGCSSY TFPKIMSPAK ATEMLIFGKK LTAGEACAQG LVTEVFPDST FQKEVWTRLK AFAKLPPNVL RISKEVIRKR EREKLHAVNA EECNVLQGRW LSDECTNAVV NFLSRKSKL // ID PECI_MOUSE STANDARD; PRT; 358 AA. AC Q9WUR2; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8) (Dodecenoyl-CoA DE delta-isomerase) (D3,D2-enoyl-CoA isomerase). GN PECI. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99348312; PubMed=10419495; RA Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.; RT "Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA RT isomerase of mammalian peroxisomes."; RL J. Biol. Chem. 274:21797-21803(1999). CC -!- FUNCTION: ABLE TO ISOMERIZE BOTH 3-CIS AND 3-TRANS DOUBLE BONDS CC INTO THE 2-TRANS FORM IN A RANGE OF ENOYL-COA SPECIES. CC -!- CATALYTIC ACTIVITY: 3-ENOYL-COA = 2-TRANS-ENOYL-COA. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL MATRIX. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE ACBP FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE ENOYL-COA CC HYDRATASE/ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF153613; AAD34174.1; -. DR HSSP; P07107; 1ACA. DR MGD; MGI:1346064; Peci. DR InterPro; IPR000582; ACBP. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00887; ACBP; 1. DR Pfam; PF00378; ECH; 1. DR PRINTS; PR00689; ACOABINDINGP. DR ProDom; PD002965; ACBP; 1. DR PROSITE; PS00880; ACBP; 1. KW Isomerase; Peroxisome. FT DOMAIN 1 88 ACBP. FT DOMAIN 116 286 ECH-LIKE. FT SITE 356 358 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 358 AA; 39479 MW; 37AB76B193C4EA21 CRC64; MRASQQDFEN ALNQVKLLKK DPGNEVKLRL YALYKQATEG TCNMPKPGML DFVNKAKWDA WNALGSLPKE TARQNYVDLV SSLSSSSEAP SQGKRGADEK ARESKDILVT SEDGITKITF NRPTKKNAIS FQMYRDIILA LKNASTDNTV MAVFTGTGDY YCSGNDLTNF TSATGGIEEA ASNGAVLLRD FVNSFIDFPK PLVAVVNGPA VGISVTLLGL FDAVFASDRA TFHTPFSQLG QSPEACSSYT FPKMMGSAKA AEMLLFGKKL TAREAWAQGL VTEVFPESTF ETEVWTRLKT YANVPPNAMR ISKELIRQNE KEKLYAVNAE ECTTLQARWL SEECMNAIMS FVSRKPKL // ID PEX8_PICAN STANDARD; PRT; 650 AA. AC Q00925; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Peroxisomal matrix protein PER1 precursor (Peroxin-8). GN PEX8 OR PER1. OS Pichia angusta (Yeast) (Hansenula polymorpha). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4905; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CBS 4732; RX MEDLINE=95050945; PubMed=7962056; RA Waterham H.R., Titorenko V.I., Haima P., Cregg J.M., Harder W., RA Veenhuis M.; RT "The Hansenula polymorpha PER1 gene is essential for peroxisome RT biogenesis and encodes a peroxisomal matrix protein with both RT carboxy- and amino-terminal targeting signals."; RL J. Cell Biol. 127:737-749(1994). CC -!- FUNCTION: ESSENTIAL FOR PEROXISOME BIOGENESIS. MAY PLAY A ROLE IN CC TRIGGERING THE PROTEIN IMPORT COMPETENCE OF INDIVIDUAL CC PEROXISOMES. IT MAY INTERACT WITH PER8 (PEX10). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; MATRIX. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z30206; CAA82928.1; -. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Peroxisome; Transit peptide. FT TRANSIT 1 ? MICROBODY. FT CHAIN ? 650 PEROXISOMAL MATRIX PROTEIN PER1. FT SITE 648 650 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 650 AA; 74122 MW; A9AC534204F50C7D CRC64; MQPWYHKLGR QGRQLAEQWQ TDAEPWGVAT PTPLDYLFDE LTAPKPSTTP DKVLSYLAYY YPKLKNENNV ELLTLCFLRC PLFFNDAQLV SFSDNYRVIE CFKYIMDKKF QISQPTLPFY RFYNALFGAL AKVVADSACA WKVVPVAVGC LLSVDSRNDY DRYPEHFQLI ATVDAKLVDM AAHTLERSMD GPLSNDLLCL NVVALSCVQD KLVDSQLLRI LRVRSDILKI LTELTFNSPY GLDNGRLLTK SNANTPIVVR HLNRISFLFT KLTSIHPKIV LLADDLDLIL NRIQTFSESV LSIPNPSETQ WSTLRVVLFA QVMMFEGIMA RFFQINNHSL NSTVLPTLCR KILTTLFNFN FVVDRIGTGG FESYNFVYAS CLSTLTSYDI PTAETLIKCW TSSVAFKKVD NSATERGKLL FDLQFIENVV NLVSDSLKFE FIIPIVQDLI GNAQDQAVLE SAHSVMLKYF TSVDTYNEAQ LVDYTNNVKH VGAQLIDYLT LSLDQFPARL SLSQVGIIVE TLAKITFPDT AVHECDPELY RELLLLVYNR CLVATSEELP NVQAPPKTRH GAFTSLLIRI LPLIPFDEYQ SWLERTLSLA FRTVGDERTY LLDLLWDSIL GTNRHYPQKG YVGIQWWYEH VNESQEKAKL // ID PEX8_PICPA STANDARD; PRT; 713 AA. AC Q01962; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Peroxisomal protein PER3 precursor (Peroxin-8). GN PEX8 OR PER3. OS Pichia pastoris (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4922; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95256269; PubMed=7738036; RA Liu H., Tan X., Russell K.A., Veenhuis M., Cregg J.M.; RT "PER3, a gene required for peroxisome biogenesis in Pichia pastoris, RT encodes a peroxisomal membrane protein involved in protein import."; RL J. Biol. Chem. 270:10940-10951(1995). CC -!- FUNCTION: ESSENTIAL COMPONENT OF THE MACHINERY REQUIRED FOR THE CC IMPORT OF BOTH PTS1 AND PTS2 (AND PERHAPS ALL) PEROXISOMAL MATRIX CC PROTEINS. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; MATRIX (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L40485; AAC41653.1; -. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Peroxisome; Transit peptide. FT TRANSIT 1 ? MICROBODY. FT CHAIN ? 713 PEROXISOMAL PROTEIN PER3. FT SITE 711 713 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 713 AA; 81007 MW; AABB586B3397C971 CRC64; MYRLGSQGRS IQSQLQNGDS SSGRPLQLQG TGMREAQRIP QQLDYLLAEI ISPNEDTNVI GYLAYYYPKL KNEQNVALLT DFFLRCPTYF SHSNVVSLRN NYPVMEAFNY IMTTKFKVSQ PTVPFYRFYA AVLASLLNCE KTDPSHHWKL IPILTGVLLS IKGRDDVELY PDHSRSIKGS DTAVAQLLQR CLLRFYQSGD ARSYDLNALV IISMSCALDY VEDDTIKKIL YCFNYTRAII DLIYYSPYGL NDSDIPLLSD SSVNSQSFDQ LLNNNPALKH LNRLSFLFER TVKLNDGSIQ SNLNDIDISL NKMQSFSEKL SKKISVLDDD SSKGVGQLLR QCLYASIIIH QAILTTFFQL DNADYTKYFL PSFSRKILSI LFNLFFIVDR IGTGGFQPYN FVYLTCLQGI IQYDMKTAES LVKTFTTGIN YSSLKDSEVA RAKLLFTLNL MEQIVNICSD DLRLELIVPL VEDLVNNKNA CVDIHNHVFK SIFESAHSVI LKFFTVVDSS VKNVDYETNV TLVSEKIIPY LTLVIDQFPE FLSINQLDIA IETISRTVFP DSPIYSYDKN ISSMFLNVLF NKCLTVDNDE LVELPAIEAV VAPKNDEENN TSDAQDGGPK ELQSLNDLKS RRSALISALI SVFPLIPVKD YTKWLSIAFY DLIVATPERT ERAFLQERLW DCVVGTNKYD PQKGNLGIMW WYENVNAQST AKL // ID PEX8_YEAST STANDARD; PRT; 589 AA. AC P53248; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Peroxisomal protein PAS6 (Peroxin-8). GN PEX8 OR PAS6 OR YGR077C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RA Wedler H., Scharfe M., Wedler E., Wambutt R.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR PEROXISOME ASSEMBLY. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; MATRIX (POTENTIAL). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z72862; CAA97079.1; -. DR SGD; S0003309; PEX8. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Peroxisome. FT SITE 587 589 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 589 AA; 68165 MW; 7683417142F81701 CRC64; MFDHDVEYLI TALSSETRIQ YDQRLLDEIA ANVVYYVPRV KSPDTLYRLV GALFRSQFIV QLPPLRLLHI VKDVFLWKLE VSEPTLPISK FYLVWNAVFE SHRATWNLSQ LMVLDGVLVT YPSFKQLNNA YFIDESSNKT ALYYRNWKLQ LFSPIWAQLW NTAIVRANLS IQHCLLIALA LLFNQSNRSA LLHGVDVSWN LVTEKLLDLL EEYVHGIVQP MEIFSTDSVL STNLNHLASC LTSSITRSNE ATLVNSVRKL ERICRYLSDT VASLKEQQLD FKFQNVFILI ILALKELSAM NMTILPNHKD TFYSMICLSL FHVHVLTQKI GTVGFPSYDY VYDNLVTYFI VMDDLSKITT VLELMKRNNT KQDPNKLVFY INFLNKITNY YGCRIRLPFI TEFIEPLLHF DVFFSGKTGN TLDIEIKESI HTLTITVLSI DSSYSSQVAQ WQVSRILVYL KMSMDQFIAG KLSANQILLI FGHLSTQLPS LHNYNKHLLR DSLHETYIRI VNVKNPEKKN VLIECLIVQI AFINNPHHLI GWLNICLQLI NTHNKKLLQQ LWEMVSSLES SLAIDWWYTT VLSSQSSKL // ID PMPA_CANBO STANDARD; PRT; 166 AA. AC P14292; DT 01-JAN-1990 (Rel. 13, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Peroxisomal membrane protein A (PMP20). GN PMPA. OS Candida boidinii (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5477; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-25. RC STRAIN=ATCC 32195; RX MEDLINE=89340488; PubMed=2760051; RA Garrard L.J., Goodman J.M.; RT "Two genes encode the major membrane-associated protein of methanol- RT induced peroxisomes from Candida boidinii."; RL J. Biol. Chem. 264:13929-13937(1989). RN [2] RP CROSS-REACTIVITY WITH ASP F 3. RX MEDLINE=98074056; PubMed=9412580; RA Hemmann S., Blaser K., Crameri R.; RT "Allergens of Aspergillus fumigatus and Candida boidinii share IgE- RT binding epitopes."; RL Am. J. Respir. Crit. Care Med. 156:1956-1962(1997). CC -!- FUNCTION: ITS FUNCTION IS VERY LIKELY TO BE RELATED TO THE CC METABOLISM OF METHANOL. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL; MEMBRANE-ASSOCIATED. CC -!- INDUCTION: BY METHANOL. CC -!- MISCELLANEOUS: SHARE COMMON IGE-BINDING EPITOPES WITH ALLERGEN ASP CC F 3 OF ASPERGILLUS FUMIGATUS. CC -!- SIMILARITY: BELONGS TO THE PEROXIREDOXIN 2 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04984; AAA34357.1; -. DR PIR; A32646; A32646. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Methanol utilization; Membrane; Peroxisome; Multigene family. FT INIT_MET 0 0 FT SITE 164 166 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 166 AA; 17873 MW; CBA0781112FBD62A CRC64; APIKRGDRFP TTDDVYYIPP EGGEPGPLEL SKFVKTKKFV VVSVPGAFTP PCTEQHLPGY IKNLPRILSK GVDFVLVISQ NDPFVLKGWK KELGAADAKK LVFVSDPNLK LTKKLGSTID LSAIGLGTRS GRLALIVNRS GIVEYAAIEN GGEVDVSTAQ KIIAKL // ID PMVK_HUMAN STANDARD; PRT; 191 AA. AC Q15126; DT 15-JUL-1998 (Rel. 36, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Phosphomevalonate kinase (EC 2.7.4.2) (PMKASE). GN PMVK OR PMKI. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=96291886; PubMed=8663599; RA Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F., RA Gibson K.M.; RT "Molecular cloning of human phosphomevalonate kinase and RT identification of a consensus peroxisomal targeting sequence."; RL J. Biol. Chem. 271:17330-17334(1996). RN [2] RP SEQUENCE OF 32-191 FROM N.A. RX MEDLINE=99208737; PubMed=10191291; RA Olivier L.M., Chambliss K.L., Gibson K.M., Krisans S.K.; RT "Characterization of phosphomevalonate kinase: chromosomal RT localization, regulation, and subcellular targeting."; RL J. Lipid Res. 40:672-679(1999). CC -!- CATALYTIC ACTIVITY: ATP + (R)-5-PHOSPHOMEVALONATE = ADP + CC (R)-5-DIPHOSPHOMEVALONATE. CC -!- PATHWAY: CHOLESTEROL BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: HEART, LIVER, SKELETAL MUSCLE, KIDNEY, AND CC PANCREAS. LOWER LEVEL IN BRAIN, PLACENTA, AND LUNG. CC -!- INDUCTION: BY STEROL. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L77213; AAC37593.1; -. DR EMBL; AF026069; AAC60791.1; -. KW Transferase; Kinase; Sterol biosynthesis; Cholesterol biosynthesis; KW Peroxisome. FT INIT_MET 0 0 BY SIMILARITY. FT SITE 189 191 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 191 AA; 21864 MW; 282EB6D0723CC492 CRC64; APLGGAPRLV LLFSGKRKSG KDFVTEALQS RLGADVCAVL RLSGPLKEQY AQEHGLNFQR LLDTSTYKEA FRKDMIRWGE EKRQADPGFF CRKIVEGISQ PIWLVSDTRR VSDIQWFREA YGAVTQTVRV VALEQSRQQR GWVFTPGVDD AESECGLDNF GDFDWVIENH GVEQRLEEQL ENLIEFIRSR L // ID PTE1_HUMAN STANDARD; PRT; 319 AA. AC O14734; O15261; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal acyl-coenzyme A thioester hydrolase 1 (EC 3.1.2.2) DE (Peroxisomal long-chain acyl-coA thioesterase 1) (HIV-Nef associated DE acyl coA thioesterase) (Thioesterase II) (hTE). GN PTE1 OR HNAACTE. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97445158; PubMed=9299485; RA Watanabe H., Shiratori T., Shoji H., Miyatake S., Okazaki Y., RA Ikuta K., Sato T., Saito T.; RT "A novel acyl-CoA thioesterase enhances its enzymatic activity by RT direct binding with HIV Nef."; RL Biochem. Biophys. Res. Commun. 238:234-239(1997). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Lymphoid; RX MEDLINE=97298085; PubMed=9153233; RA Liu L.X., Margottin F., LeGall S., Schwartz O., Selig L., Benarous R., RA Benichou S.; RT "Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with RT Nef-mediated CD4 down-regulation."; RL J. Biol. Chem. 272:13779-13785(1997). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Muscle; RX MEDLINE=99194760; PubMed=10092594; RA Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.; RT "Identification of peroxisomal acyl-CoA thioesterases in yeast and RT humans."; RL J. Biol. Chem. 274:9216-9223(1999). CC -!- FUNCTION: MAY PLAY A ROLE IN FATTY ACID OXIDATION RATHER THAN CC FORMATION OF FATTY ACIDS. MAY MEDIATE NEF-INDUCED DOWN-REGULATION CC OF CD4. CC -!- CATALYTIC ACTIVITY: PALMITOYL-COA + H(2)O = COA + PALMITATE. CC -!- SUBUNIT: INTERACTS WITH HIV-1 NEF. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE C/M/P THIOESTER HYDROLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF014404; AAB71665.1; -. DR EMBL; X86032; CAA60024.1; -. DR EMBL; AF124264; AAD27616.1; -. DR HSSP; P23911; 1C8U. DR InterPro; IPR003703; Acyl_CoA_thio. DR Pfam; PF02551; Acyl_CoA_thio; 1. KW Hydrolase; Serine esterase; Peroxisome. FT ACT_SITE 78 78 BY SIMILARITY. FT ACT_SITE 232 232 BY SIMILARITY. FT SITE 317 319 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 291 293 LWR -> VWS (IN REF. 2). FT CONFLICT 319 319 L -> R (IN REF. 2). SQ SEQUENCE 319 AA; 35914 MW; 8345C6E5EABF3326 CRC64; MSSPQAPEDG QGCGDRGDPP GDLRSVLVTT VLNLEPLDED LFRGRHYWVP AKRLFGGQIV GQALVAAAKS VSEDVHVHSL HCYFVRAGDP KLPVLYQVER TRTGSSFSVR SVKAVQHGKP IFICQASFQQ AQPSPMQHQF SMPTVPPPEE LLDCETLIDQ YLRDPNLQKR YPLALNRIAA QEVPIEIKPV NPSPLSQLQR MEPKQMFWVR ARGYIGEGDM KMHCCVAAYI SDYAFLGTAL LPHQWQHKVH FMVSLDHSMW FHAPFRADHW MLYECESPWA GGSRGLVHGR LWRQDGVLAV TCAQEGVIRV KPQVSESKL // ID PTE1_MOUSE STANDARD; PRT; 320 AA. AC P58137; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal acyl-coenzyme A thioester hydrolase 1 (EC 3.1.2.2) DE (Peroxisomal long-chain acyl-coA thioesterase 1). GN PTE1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RA Strausberg R.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY PLAY A ROLE IN FATTY ACID OXIDATION RATHER THAN CC FORMATION OF FATTY ACIDS (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: PALMITOYL-COA + H(2)O = COA + PALMITATE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE C/M/P THIOESTER HYDROLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; BC005792; AAH05792.1; -. KW Hydrolase; Serine esterase; Peroxisome. FT ACT_SITE 79 79 BY SIMILARITY. FT ACT_SITE 233 233 BY SIMILARITY. FT SITE 318 320 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 320 AA; 35827 MW; 94F6AFCFEEE2FA23 CRC64; MSAPEGLGDA HGDADRGDLS GDLRSVLVTS VLNLEPLDED LYRGRHYWVP TSQRLFGGQI MGQALVAAAK SVSEDVHVHS LHCYFVRAGD PKVPVLYHVE RIRTGASFSV RAVKAVQHGK AIFICQASFQ QMQPSPLQHQ FSMPSVPPPE DLLDHEALID QYLRDPNLHK KYRVGLNRVA AQEVPIEIKV VNPPTLTQLQ ALEPKQMFWV RARGYIGEGD IKMHCCVAAY ISDYAFLGTA LLPHQSKYKV NFMASLDHSM WFHAPFRADH WMLYECESPW AGGSRGLVHG RLWRRDGVLA VTCAQEGVIR LKPQVSESKL // ID PTE1_YEAST STANDARD; PRT; 349 AA. AC P41903; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal acyl-coenzyme A thioester hydrolase 1 (EC 3.1.2.2) DE (Peroxisomal long-chain acyl-coA thioesterase 1). GN TES1 OR PTE1 OR YJR019C OR J1456. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DH484; RA Hani J., Stumpf G., Domdey H.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / FY1679; RA de Haan M., Smits P.H.M., Grivell L.A.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=99194760; PubMed=10092594; RA Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.; RT "Identification of peroxisomal acyl-CoA thioesterases in yeast and RT humans."; RL J. Biol. Chem. 274:9216-9223(1999). CC -!- FUNCTION: MAY PLAY A ROLE IN FATTY ACID OXIDATION RATHER THAN CC FORMATION OF FATTY ACIDS. CC -!- CATALYTIC ACTIVITY: PALMITOYL-COA + H(2)O = COA + PALMITATE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE C/M/P THIOESTER HYDROLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X85972; CAA59960.1; -. DR EMBL; X87611; CAA60943.1; -. DR EMBL; Z49519; CAA89543.1; -. DR EMBL; AF124265; AAD27617.1; -. DR SGD; S0003780; TES1. DR InterPro; IPR003703; Acyl_CoA_thio. DR Pfam; PF02551; Acyl_CoA_thio; 1. KW Hydrolase; Serine esterase; Peroxisome. FT ACT_SITE 259 259 BY SIMILARITY. FT SITE 347 349 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 349 AA; 40259 MW; F1B5A51C9A46783E CRC64; MSASKMAMSN LEKILELVPL SPTSFVTKYL PAAPVGSKGT FGGTLVSQSL LASLHTVPLN FFPTSLHSYF IKGGDPRTKI TYHVQNLRNG RNFIHKQVSA YQHDKLIFTS MILFAVQRSK EHDSLQHWET IPGLQGKQPD PHRYEEATSL FQKEVLDPQK LSRYASLSDR FQDATSMSKY VDAFQYGVME YQFPKDMFYS ARHTDELDYF VKVRPPITTV EHAGDESSLH KHHPYRIPKS ITPENDARYN YVAFAYLSDS YLLLTIPYFH NLPLYCHSFS VSLDHTIYFH QLPHVNNWIY LKISNPRSHW DKHLVQGKYF DTQSGRIMAS VSQEGYVVYG SERDIRAKF // ID PTE2_HUMAN STANDARD; PRT; 421 AA. AC P49753; Q9NUX4; DT 01-OCT-1996 (Rel. 34, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal acyl-coenzyme A thioester hydrolase 2 (EC 3.1.2.2) DE (Peroxisomal long-chain acyl-coA thioesterase 2) (ZAP128). GN PTE2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20403902; PubMed=10944470; RA Jones J.M., Gould S.J.; RT "Identification of PTE2, a human peroxisomal long-chain acyl-CoA RT thioesterase."; RL Biochem. Biophys. Res. Commun. 275:233-240(2000). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RA Isogai T., Ota T., Hayashi K., Sugiyama T., Otsuki T., Suzuki Y., RA Nishikawa T., Nagai K., Sugano S., Aotsuka S., Yoshikawa Y., RA Matsunawa H., Ishii S., Kawai Y., Saito K., Yamamoto J., Wakamatsu A., RA Nakamura Y., Nagahari K., Masuho Y., Sasaki N.; RT "NEDO human cDNA sequencing project."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Uterus, and Lung; RA Strausberg R.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 119-421 FROM N.A. RC TISSUE=Brain; RX MEDLINE=95319502; PubMed=7596406; RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., RA Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., RA Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., RA Pinessi L., Nee L., Chumakov I., Pollen D., Brookes A., RA Sanseau P., Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L., RA Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., RA Rommens J.M., St George-Hyslop P.H.; RT "Cloning of a gene bearing missense mutations in early-onset familial RT Alzheimer's disease."; RL Nature 375:754-760(1995). CC -!- CATALYTIC ACTIVITY: PALMITOYL-COA + H(2)O = COA + PALMITATE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE C/M/P THIOESTER HYDROLASE FAMILY. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS TO THAT SHOWN DUE TO FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY005822; AAF97985.1; -. DR EMBL; AK001939; BAA91989.1; ALT_INIT. DR EMBL; BC006335; AAH06335.1; -. DR EMBL; BC006500; AAH06500.1; ALT_INIT. DR EMBL; L40401; AAC42007.1; ALT_FRAME. DR InterPro; IPR000379; Est_lip_thioest_actsite. KW Hydrolase; Serine esterase; Peroxisome. FT SITE 419 421 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 105 105 E -> V (IN REF. 2). FT CONFLICT 266 266 R -> H (IN REF. 4). FT CONFLICT 392 392 A -> V (IN REF. 3; AAH06335). FT CONFLICT 413 413 R -> H (IN REF. 3; AAH06335 AND REF. 4). SQ SEQUENCE 421 AA; 46330 MW; C24BED9111A28710 CRC64; MAATLILEPA GRCCWDEPVR IAVRGLAPEQ PVTLRASLRD EKGALFQAHA RYRADTLGEL DLERAPALGG SFAGLEPMGL LWALEPEKPL VRLVKRDVRT PLAVELEVLD GHDPDPGRLL CQTRHERYFL PPGVRREPVR VGRVRGTLFL PPEPGPFPGI VDMFGTGGGL LEYRASLLAG KGFAVMALAY YNYEDLPKTM ETLHLEYFEE AMNYLLSHPE VKGPGVGLLG ISKGGELCLS MASFLKGITA AVVINGSVAN VGGTLRYKGE TLPPVGVNRN RIKVTKDGYA DIVDVLNSPL EGPDQKSFIP VERAESTFLF LVGQDDHNWK SEFYANEACK RLQAHGRRKP QIICYPETGH YIEPPYFPLC RASLHALVGS PIIWGGEPRA HAMAQVDAWK QLQTFFHKHL GGREGTIPSK V // ID PTE2_MOUSE STANDARD; PRT; 432 AA. AC Q9QYR7; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Peroxisomal acyl-coenzyme A thioester hydrolase 2 (EC 3.1.2.2) DE (Peroxisomal long-chain acyl-coA thioesterase 2) (PTE-Ia). GN PTE2 OR PTE1A. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6; RX MEDLINE=20036578; PubMed=10567408; RA Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., RA Thomas Svensson L., Alexson S.E.H.; RT "Peroxisome proliferator-induced long chain acyl-CoA thioesterases RT comprise a highly conserved novel multi-gene family involved in lipid RT metabolism."; RL J. Biol. Chem. 274:34317-34326(1999). CC -!- CATALYTIC ACTIVITY: PALMITOYL-COA + H(2)O = COA + PALMITATE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE C/M/P THIOESTER HYDROLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF180804; AAF13873.1; -. DR EMBL; AF180802; AAF13873.1; JOINED. DR EMBL; AF180803; AAF13873.1; JOINED. DR InterPro; IPR000379; Est_lip_thioest_actsite. KW Hydrolase; Serine esterase; Peroxisome. FT SITE 430 432 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 432 AA; 47489 MW; BF5888C59C015359 CRC64; MHAFTTQNPN RMAPTVILEP AGGCLCDQPV HIAVRGLAPE QPVTLRSVLR DEKGALFRAH ARYRADSHGE LDLARTPALG GSFSGLEPMG LLWAMEPDRP FWRLIKRDVQ TPFVVELEVL DGHEPDGGQR LARAVHERHF MAPGVRRVPV REGRVRATLF LPPGTGPFPG IIDLFGIGSG LLEYRASLLA GKGFAVMALA YNNYEDLPKD MDIIHLEYFE EAVTYLLSHP QVTGSGVGVL GISKGGELGF AMASFLKNIT AAVIINGSIS NIGGNLQYKD ETVPSVGINT KRVKRTKDGL KDIVDLLNNP LEGPDQKSLI PVERSDTAFL FLVGQDDHNW KSEFYAREAS KRLQAHGKEK PQIICYPETG HHIEPPYFPL CKASLNSLVG GPVIWGGEPR AHAMAQVDAW QQLQTFFHNH LDGKKKTIPA KL // ID SPYA_FELCA STANDARD; PRT; 414 AA. AC P41689; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine--pyruvate aminotransferase, mitochondrial precursor DE (EC 2.6.1.51) (SPT) (Alanine--glyoxylate aminotransferase) DE (EC 2.6.1.44) (AGT). GN AGXT OR AGT1. OS Felis silvestris catus (Cat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Carnivora; Fissipedia; Felidae; Felis. OX NCBI_TaxID=9685; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=94222101; PubMed=8168541; RA Lumb M.J., Purdue P.E., Danpure C.J.; RT "Molecular evolution of alanine/glyoxylate aminotransferase 1 RT intracellular targeting. Analysis of the feline gene."; RL Eur. J. Biochem. 221:53-62(1994). CC -!- FUNCTION: DUAL METABOLIC ROLES OF GLUCONEOGENESIS (IN THE CC MITOCHONDRIA) AND GLYOXYLATE DETOXIFICATION (IN THE PEROXISOMES). CC -!- CATALYTIC ACTIVITY: L-SERINE + PYRUVATE = 3-HYDROXYPYRUVATE + CC L-ALANINE. CC -!- CATALYTIC ACTIVITY: L-ALANINE + GLYOXYLATE = PYRUVATE + GLYCINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (>90%) AND PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75923; CAA53527.1; -. DR InterPro; IPR000192; Aminotransf_class_V. DR Pfam; PF00266; aminotran_5; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Peroxisome; KW Mitochondrion; Transit peptide; Alternative initiation. FT TRANSIT 1 23 MITOCHONDRION (BY SIMILARITY). FT CHAIN 24 414 SERINE--PYRUVATE AMINOTRANSFERASE, FT MITOCHONDRIAL ISOFORM. FT CHAIN 23 414 SERINE--PYRUVATE AMINOTRANSFERASE, FT PEROXISOMAL ISOFORM. FT INIT_MET 23 23 FOR PEROXISOMAL ISOFORM. FT BINDING 231 231 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT SITE 412 414 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). SQ SEQUENCE 414 AA; 45507 MW; 0D1B01E0E9A199B3 CRC64; MFRALARASA TLGPQVAGWA RTMATCQLLV APPEALLRPL SIPNRLLLGP GPSNLAPRVL VAGGKQMIGH MHKEMFQIMD DIKQGIQYVF QTKNPLTLAI SGSGHCALEA ALFNILEPGD PFLVGVNGIW GQRAADIGER IGARVHPMIK DPGNHYTLQE LEEALAQHKP VLLFLTQGES SSGVLQPLDG YGELCHRYNC LLLVDSVASL CGTPIYMDQQ GIDVLYSGSQ KVLNSPPGTS LISFSDKAKN KIYTRKTKPV SFYLDMKWLA NIWGCDGKPR IYHHTTPVVS LYSLRESLAL IAEQGLENSW RQHREVTAYL HGRLQGLGLQ LFVKDPALRL PTVTTVAVPA GYDWRDIVNY VMDHFDIEIT GGLGPSMGKV LRIGLLGCNA TRENVDRVIQ ALQEALQRCS RNKL // ID SPYA_RABIT STANDARD; PRT; 392 AA. AC P31030; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Serine--pyruvate aminotransferase (EC 2.6.1.51) (SPT) (Alanine-- DE glyoxylate aminotransferase) (EC 2.6.1.44) (AGT). GN AGXT OR AGT1. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=92339467; PubMed=1339350; RA Purdue P.E., Lumb M.J., Danpure C.J.; RT "Molecular evolution of alanine/glyoxylate aminotransferase 1 RT intracellular targeting. Analysis of the marmoset and rabbit genes."; RL Eur. J. Biochem. 207:757-766(1992). RN [2] RP MICROBODY TARGETING SIGNAL. RX MEDLINE=96021280; PubMed=7559790; RA Motley A., Lumb M.J., Oatey P.B., Jennings P.R., de Zoysa P.A., RA Wanders R.J.A., Tabak H.F., Danpure C.J.; RT "Mammalian alanine/glyoxylate aminotransferase 1 is imported into RT peroxisomes via the PTS1 translocation pathway. Increased degeneracy RT and context specificity of the mammalian PTS1 motif and implications RT for the peroxisome-to-mitochondrion mistargeting of AGT in primary RT hyperoxaluria type 1."; RL J. Cell Biol. 131:95-109(1995). CC -!- CATALYTIC ACTIVITY: L-SERINE + PYRUVATE = 3-HYDROXYPYRUVATE + CC L-ALANINE. CC -!- CATALYTIC ACTIVITY: L-ALANINE + GLYOXYLATE = PYRUVATE + GLYCINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84647; AAA31158.1; -. DR PIR; S24155; S24155. DR InterPro; IPR000192; Aminotransf_class_V. DR Pfam; PF00266; aminotran_5; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Peroxisome. FT BINDING 209 209 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT SITE 390 392 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 392 AA; 43148 MW; 5261DD14564582D3 CRC64; MASRQLLVAP PEALRKPLCT PHRLLLGPGP SNLPPRVLAA GGLQMIGHMH EEMYQVMDEI KQGIQYAFQT RNALTLAVSG SGHCALETAL FNLLEPGDAF LVGANGIWGQ RAAEVGERIG ARVHPMIKDP GSHYTLQEVE ECLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL LVDSVASLGG APIYMDQQGI DVLYSGSQKA LNAPPGTSLI SFSDKAKSKI YARKTKPFSF YMDVQLLANI WGCDGKPRMY HHTTPVIGIF ALRESLALLV EQGLEKSWQR HREVAQHLYR RLQELGLQLF VKDPALRLPT VTTVIVPASY RWRDIVSYVM HHFGIEITGG LGPSADKVLR IGLLGCNATR ENVDRLATAL REALQHCAQS QL // ID THIB_CANTR STANDARD; PRT; 402 AA. AC Q04677; DT 01-OCT-1993 (Rel. 27, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Acetyl-CoA acetyltransferase IB (EC 2.3.1.9) (Peroxisomal DE acetoacetyl-CoA thiolase) (Thiolase IB). GN PACTB. OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5482; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-16; 208-232 AND 279-289. RX MEDLINE=93130927; PubMed=1362382; RA Kurihara T., Ueda M., Kanayama N., Kondo J., Teranishi Y., Tanaka A.; RT "Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast, RT Candida tropicalis."; RL Eur. J. Biochem. 210:999-1005(1992). CC -!- CATALYTIC ACTIVITY: 2 ACETYL-COA = COA + ACETOACETYL-COA. CC -!- PATHWAY: FIRST STEP IN BIOSYNTHESIS OF POLY BETA-HYDROXYBUTYRATE. CC -!- SUBUNIT: MULTIMERIC (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE THIOLASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13471; BAA02716.1; -. DR PIR; S28144; S28144. DR HSSP; P27796; 1PXT. DR InterPro; IPR002155; Thiolase. DR Pfam; PF00108; thiolase; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00099; THIOLASE_3; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Transferase; Acyltransferase; Peroxisome. FT INIT_MET 0 0 FT ACT_SITE 90 90 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 382 382 BASE (BY SIMILARITY). FT SITE 400 402 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 402 AA; 41799 MW; 599B4F2D195F6757 CRC64; TLPPVYIVST ARTPIGSFQG SLSSLTYSDL GAHAVKAALA KVPQIKPQDV DEIVFGGVLQ ANVGQAPARQ VALKAGLPDS IIASTINKVC ASGMKAVIIG AQNIICGTSD IVVVGGAESM SNTPYYLPSA RSGARYGDAV MVDGVQKDGL LDVYEEKLMG VAAEKCAKDH GFSREDQDNF AINSYKKAGK ALSEGKFKSE IAPVTIKGFR GKPDTVIEND EEIGKFNEDR LKSARTVFQK ENGTVTAPNA SKLNDGGAAL VLVSEAKLKQ LGLKPLAKIS GWGEAARTPF DFTIAPALAV PKAVKHAGLT VDRVDFFELN EAFSVVGLAN AELVKIPLEK LNVYGGAVAM GHPLGCSGAR IIVTLLSVLT QEGGRFGAAG VCNGGGGASA IVIEKIDSDA KL // ID URIC_ARATH STANDARD; PRT; 309 AA. AC O04420; O64848; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase) (Nodulin 35 homolog). GN AT2G26230 OR T1D16.13. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. LANDSBERG ERECTA; RA Marchfelder A., Binder S., Brennicke A.; RT "A nodulin-35 homologue is encoded in the Arabidopsis genome."; RL Trends Plant Sci. 2:167-168(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20083487; PubMed=10617197; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., VanAken S.E., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11120; CAA72005.1; -. DR EMBL; AC004484; AAC14527.1; -. DR Mendel; 16778; ARAth;1087;mn16778. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 307 309 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 11 11 E -> D (IN REF. 2). SQ SEQUENCE 309 AA; 34895 MW; 56D58B85CACB1593 CRC64; MAQEADGIRL EQRHGKARVR VGRVWRHAHD GSHHFVEWNV SISLLSHCLS SYRLDDNSDI VATDTIKNTV YVKAKECGDR LSVEEFAILI GKHFCSFYPQ VFTAIVNIIE KPWERVSIDG KPHLHGFKLG SENHTTEARV EKSGALNLTS GIGGLALLKT TQSGFERFVR DKYTILPETR ERMLATEVNA SWRYSYESVA SIPTKGLYFS EKFMDVKKVL MDTFFGPPET GVYSPSVQRT LYLMGSAVLK RFADVSSIHL KMPNIHFLPV NLSTKENPSM VKFKDDVYLP TDEPHGSIEA TLSRITSKL // ID URIC_ASPFL STANDARD; PRT; 301 AA. AC Q00511; DT 01-DEC-1992 (Rel. 24, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UAZ OR UOX. OS Aspergillus flavus. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5059; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=ATCC 20047; RX MEDLINE=92235086; PubMed=1339455; RA Legoux R., Delpech B., Dumont X., Guillemot J.C., Ramond P., RA Shire D., Caput D., Ferrara P., Loison G.; RT "Cloning and expression in Escherichia coli of the gene encoding RT Aspergillus flavus urate oxidase."; RL J. Biol. Chem. 267:8565-8570(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=98025064; PubMed=9360612; RA Colloc'H N., el Hajji M., Bachet B., L'Hermite G., Schiltz M., RA Prange T., Castro B., Mornon J.P.; RT "Crystal structure of the protein drug urate oxidase-inhibitor RT complex at 2.05-A resolution."; RL Nat. Struct. Biol. 4:947-952(1997). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61766; CAA43896.1; -. DR EMBL; X61765; CAA43895.1; -. DR EMBL; A17664; CAA01345.1; -. DR PIR; S22867; S22867. DR PIR; S22868; S22868. DR PIR; A38097; A38097. DR PDB; 1UOX; 16-SEP-98. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism; Acetylation; KW 3D-structure. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT SITE 299 301 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 301 AA; 34109 MW; 3068345BA1ABA392 CRC64; SAVKAARYGK DNVRVYKVHK DEKTGVQTVY EMTVCVLLEG EIETSYTKAD NSVIVATDSI KNTIYITAKQ NPVTPPELFG SILGTHFIEK YNHIHAAHVN IVCHRWTRMD IDGKPHPHSF IRDSEEKRNV QVDVVEGKGI DIKSSLSGLT VLKSTNSQFW GFLRDEYTTL KETWDRILST DVDATWQWKN FSGLQEVRSH VPKFDATWAT AREVTLKTFA EDNSASVQAT MYKMAEQILA RQQLIETVEY SLPNKHYFEI DLSWHKGLQN TGKNAEVFAP QSDPNGLIKC TVGRSSLKSK L // ID URIC_CANLI STANDARD; PRT; 308 AA. AC P34798; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase II clone PCCLNUO-01 (EC 1.7.3.3) (Urate oxidase). OS Canavalia lineata. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Canavalia. OX NCBI_TaxID=28957; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Root nodules; RA Bang K.H., An C.S.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS IS A SUBUNIT OF THE NODULE SPECIFIC URICASE. CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76286; CAA53904.1; -. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Nodulation; Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 306 308 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 308 AA; 34943 MW; 2968988B6FA1993D CRC64; MAKEIVGGFK FDQRHGKERV QVARVWKTKQ GWYFIVEWRV GNSLLSDCVN SYVRDDNSDI VATDTMKNTV YAKAKECSEI LSVEDFAILL AKHFISFYKQ VTAAIVNIVE KPWERVSVDG QPHEHGFKLG SERHTAEAIV QKSGALQLTS GIEGLSLLKT TKSGFEGFIR DKYTALPETH ERMLATEVTA LWRYSYESLY SIPQKPLYFT DKYLEVKKVL ADNFFGPPNV GVYSPSVQNT LYLMAKAALN RFPEIASIQL KMPNIHFLPV NISNKDGPIV KFEADVYLPT DEPHGSIQAS LRRLWSKL // ID URIC_DROME STANDARD; PRT; 352 AA. AC P16163; Q9VLX4; DT 01-APR-1990 (Rel. 14, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN URO OR UO OR CG7171. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=CANTON-S; TISSUE=Salivary gland; RX MEDLINE=90377201; PubMed=2118989; RA Wallrath L.L., Burnett J.B., Friedman T.B.; RT "Molecular characterization of the Drosophila melanogaster urate RT oxidase gene, an ecdysone-repressible gene expressed only in the RT malpighian tubules."; RL Mol. Cell. Biol. 10:5114-5127(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- ENZYME REGULATION: REPRESSED BY 20-HYDROXYECDYSONE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: MALPIGHIAN TUBULES. CC -!- DEVELOPMENTAL STAGE: THIRD INSTAR LARVAE AND ADULT. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X51940; CAA36203.1; -. DR EMBL; AE003618; AAF52555.1; -. DR PIR; S08676; S08676. DR PIR; A35920; A35920. DR FlyBase; FBgn0003961; Uro. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 350 352 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 114 114 R -> K (IN REF. 1). SQ SEQUENCE 352 AA; 40062 MW; 1D0E00F8AD0FC96F CRC64; MFATPLRQPA AANHQTPKNS AGMDEHGKPY QYEITDHGYG KDAVKVLHVS RNGPVHAIQE FEVGTHLKLY SKKDYYQGNN SDIVATDSQK NTVYLLAKKH GIESPEKFAL LLARHFINKY SHVEEAHVHV EAYPWQRVCQ EETRTNVNGK CENGVQGNCD FSSIDNRSLH NHAFIFTPTA LHYCDVVIRR TDPKQTVITG IKGLRVLKTT QSSFVNFVND EFRSLPDQYD RIFSTVVDCS WEYSDTENLD FLRAWQTVKN IIIRNFAGDP QVGVSSPSVQ HTLYLSERQV LDVLPQVSVI SMTMPNKHYF NFDTKPFQKI APGDNNEVFI PVDKPHGTIY AQLARKNINS HL // ID URIC_DROPS STANDARD; PRT; 345 AA. AC P22673; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN URO OR UO. OS Drosophila pseudoobscura (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7237; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AH133; RX MEDLINE=92211723; PubMed=1556745; RA Friedman T.B., Burnett J.B., Lootens S., Wallrath L.L.; RT "The urate oxidase gene of Drosophila pseudoobscura and Drosophila RT melanogaster: evolutionary changes of sequence and regulation."; RL J. Mol. Evol. 34:62-77(1992). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- ENZYME REGULATION: REPRESSED BY 20-HYDROXYECDYSONE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: MALPIGHIAN TUBULES. CC -!- DEVELOPMENTAL STAGE: THIRD INSTAR LARVAE AND ADULT. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57113; CAA40396.1; -. DR FlyBase; FBgn0012716; Dpse\Uro. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 343 345 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 345 AA; 39195 MW; 4A0B753D72680F36 CRC64; MFATPLRQPT NASGARPAVS MDGQETPFQY EITDHGYGKD AVKVLHVSRK GPVHTIQEFE VGTHLKLYSK KDYYQGNNSD IVATDSQKNT VYLLAKKYGI ESPEKFALML GQHFLNKYSH VEEAHVHVET YPWQRVCQEE TKSVNNQGQG SCNNFTSIDN RSLHNHAFIF TPTAVHYCDV VIRRTPKQTV ITGIKGLRVL KTTQSSFVNF VNDEFRSLPD QYDRIFSTVV DCSWEYSDTE TVNFSRAWQT VKNIILRNFA GDPQVGVSSP SVQHTLYLSE KQVLDVIPQV SVISMTMPNK HYFNFDTKPF QKIVPGDNNE VFIPVDKPHG TIYAQLARKN ISSHL // ID URIC_DROSU STANDARD; PRT; 339 AA. AC O44111; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase) (Fragment). GN URO OR UO. OS Drosophila subobscura (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7241; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98386758; PubMed=9720289; RA Zeng L.-W., Comeron J.M., Chen B., Kreitman M.; RT "The molecular clock revisited: the rate of synonymous vs. replacement RT change in Drosophila."; RL Genetica 102:369-382(1998). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- DEVELOPMENTAL STAGE: THIRD INSTAR LARVAE AND ADULT. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF025816; AAB87901.1; -. DR FlyBase; FBgn0021077; Dsub\Uro. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT NON_TER 1 1 FT SITE 337 339 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 339 AA; 38434 MW; 34439F6B6078DC6E CRC64; LRQPSSASNR TAASLDGQET PFQYEITDHG YGKDAVKVLH VSRKGPVHTI QEFEVGTHLK LYSKKDYYQG NNSDIVATDS QKNTVYLLAK KYGIESPEKF ALLLGQHFLN KYSHVEEAHV HVETYPWQRV CQEETKASTT VGQGSCNFSS IDNRSLHNHA FIFTPTALHY CDVVIXRQDP KQTVITGIKG LRVLKTTQSS FVNFVNDEXR SLPDQYDRIF STVVDCSWEY SDTDTVNFSR AWQQVKNIIL RNFAGDPQVG VSSPSVQHTL YLSEKQVLDV IPQVSVISMT MPNKHYFNFD TKPFQQIVPG DNNEVFIPVD KPHGTIYAQL ARKNLNSHL // ID URIC_DROVI STANDARD; PRT; 342 AA. AC P23194; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN URO OR UO. OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244; RN [1] RP SEQUENCE FROM N.A. RA Wallrath L.L.; RL Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- ENZYME REGULATION: REPRESSED BY 20-HYDROXYECDYSONE. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: MALPIGHIAN TUBULES. CC -!- DEVELOPMENTAL STAGE: THIRD INSTAR LARVAE AND ADULT. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57114; CAA40397.1; -. DR PIR; S29133; S29133. DR FlyBase; FBgn0013101; Dvir\Uro. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 340 342 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 342 AA; 38724 MW; 4DE10D5485294723 CRC64; MFATPLRQLS SLKRSGIAGQ EQAQLYEITN KGYGKDAVKV MHINRKGPVH SIQELEVGTH LKLYSNKDYM LGNNSDVVAT DSQKNTVYLL AKKHGIESPE KFALILAKHF LSTYAHVEEV HVHVEAYPWQ RMTQDVSDNI GKGYCENNCN SRSNGNCQLH NHAFIFTPTA HDYCDVILTR QDPKQTVISG IKGLRVLKTT QSSFVNFVDD EFRTLADQYD RIFSTVVECS WEYSDTESVN FLHAWETVKD IVVRNFAGDP SVGIPSPSVQ HTLYLSEKQV LDVLPQVSVV SMTMPNKHYF NFDTKPFQQL VPGENNEVFI PTDKPHGTIY AQLSRKSLKS HL // ID URIC_EMENI STANDARD; PRT; 301 AA. AC P33282; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UAZ. OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=5072; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94043132; PubMed=8226863; RA Oestreicher N., Scazzocchio C.; RT "Sequence, regulation, and mutational analysis of the gene encoding RT urate oxidase in Aspergillus nidulans."; RL J. Biol. Chem. 268:23382-23389(1993). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X72210; CAA51009.1; -. DR PIR; S36076; S36076. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 299 301 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 301 AA; 34002 MW; BA46DD84925BCD9F CRC64; MSTVAAARYG KDNVRVYKVH KDPKTGVQTV TEMTVCVLLE GEIDTSYTKA DNSVIVATDS IKNTIFILAK QNPVTPPELF GSILGTHFIN KYKHIHVAHT NIITHRWTRL NIDGKPHSHS FVRDSEETRN VQVDVTEGVG IDIKSSINKL TVLKSTGSQF WGFVRDEYTT LPEVWDRILS TDVEATWAWK RFSGLDEVRG NVPKFDETWE AARNITLKTF AEEESASVQA TMYKMGEQIL AYQPLLETVE YSLPNKHYFE IDLSWHKGLK NTGKDAEVFV PQTNPNGLIK CTVGRKSKAK L // ID URIC_MOUSE STANDARD; PRT; 302 AA. AC P25688; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UOX. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90083277; PubMed=2594778; RA Wu X., Lee C.C., Muzny D.M., Caskey C.T.; RT "Urate oxidase: primary structure and evolutionary implications."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27695; AAA40538.1; -. DR PIR; B36227; B36227. DR SWISS-2DPAGE; P25688; MOUSE. DR MGD; MGI:98907; Uox. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT INIT_MET 0 0 BY SIMILARITY. FT SITE 300 302 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 302 AA; 34908 MW; D3E5AADDB3D86520 CRC64; AHYHDNYGKN DEVEFVRTGY GKDMVKVLHI QRDGKYHSIK EVATSVQLTL RSKKDYLHGD NSDIIPTDTI KNTVHVLAKL RGIRNIETFA MNICEHFLSS FNHVTRAHVY VEEVPWKRFE KNGIKHVHAF IHTPTGTHFC EVEQMRNGPP VIHSGIKDLK VLKTTQSGFE GFLKDQFTTL PEVKDRCFAT QVYCKWRYQR RDVDFEAIWG AVRDIVLQKF AGPYDKGEYS PSVQKTLYDI QVLSLSQLPE IEDMEISLPN IHYFNIDMSK MGLINKEEVL LPLDNPYGKI TGTVKRKLPS RL // ID URIC_PAPHA STANDARD; PRT; 303 AA. AC P25689; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UOX. OS Papio hamadryas (Hamadryas baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Cercopithecidae; OC Cercopithecinae; Papio. OX NCBI_TaxID=9557; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90083277; PubMed=2594778; RA Wu X., Lee C.C., Muzny D.M., Caskey C.T.; RT "Urate oxidase: primary structure and evolutionary implications."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27694; AAA35395.1; -. DR PIR; A36227; A36227. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT INIT_MET 0 0 BY SIMILARITY. FT SITE 301 303 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 303 AA; 34811 MW; DDE7B7608507C04F CRC64; ADYHNNYKKN DELEFVRTGY GKDMVKVLHI QRDGKYHSIK EVATSVQLTL SSKKDYLHGD NSDIIPTDTI KNTVHVLAKF KGIKSIEAFG VNICEYFLSS FNHVIRAQVY VEEIPWKRLE KNGVKHVHAF IHTPTGTHFC EVEQLRSGPP VITSGIKDLK VLKTTQSGFE GFIKDQFTTL PEVKDRCFAT QVYCKWRYHQ CRDVDFEATW GTIRDLVLEK FAGPYDKGEY SPSVQKTLYD IQVLSLSRVP EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLS SRL // ID URIC_PHAVU STANDARD; PRT; 308 AA. AC P53763; O49966; DT 01-OCT-1996 (Rel. 34, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase II (EC 1.7.3.3) (Urate oxidase) (Nodule specific uricase). GN URIII. OS Phaseolus vulgaris (Kidney bean) (French bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Phaseolus. OX NCBI_TaxID=3885; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=CV. NEGRO JAMAPA; TISSUE=Root nodules; RX MEDLINE=98076184; PubMed=9414545; RA Capote-Mainez N., Sanchez F.; RT "Characterization of the common bean uricase II and its expression in RT organs other than nodules."; RL Plant Physiol. 115:1307-1317(1997). RN [2] RP SEQUENCE OF 54-308 FROM N.A. RC STRAIN=CV. TENDERGREEN; TISSUE=Root nodules; RX MEDLINE=95145644; PubMed=7843336; RA Papadopoulou K., Roussis A., Kuin H., Katinakis P.; RT "Expression pattern of uricase II gene during root nodule development RT in Phaseolus vulgaris."; RL Experientia 51:90-94(1995). RN [3] RP CHARACTERIZATION, AND INDUCTION. RC STRAIN=CV. NEGRO JAMAPA; TISSUE=Root nodules; RA Sanchez F., Campos F., Padilla J., Bonneville J.-M., Enriquez C., RA Caput D.; RT "Purification, cDNA cloning, and developmental expression of the RT nodule-specific uricase from Phaseolus vulgaris L."; RL Plant Physiol. 84:1143-1147(1987). CC -!- FUNCTION: THIS IS A SUBUNIT OF THE NODULE SPECIFIC URICASE. CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN THE UNINFECTED CC CELLS OF THE CENTRAL TISSUE OF THE ROOT NODULE. ALSO EXPRESSED CC IN THE NODULE PARENCHYMA CELLS AND VASCULAR TISSUE, IN THE CC ROOTS, STEMS AND LEAVES OF UNINFECTED ADULT PLANTS, AND IN THE CC COTYLEDONS, ROOTS AND HYPOCOTYLS OF DEVELOPING SEEDLINGS. CC LOCALIZED TO THE METAXYLEM PARENCHYMA CELLS AND PHLOEM FIBERS OF CC DEVELOPING ROOTS. CC -!- DEVELOPMENTAL STAGE: DETECTED IN COTYLEDONS AND ROOTS AT 1 DAY CC POSTIMBIBITION, REACHING A MAXIMUM AT 4 DAYS POSTIMBIBITION. CC HYPOCOTYL LEVELS ARE CONSTANT FROM 3 TO 10 DAYS POSTIMBIBITION. CC -!- INDUCTION: IN ROOT NODULES AFTER INFECTION BY RHIZOBIUM. NODULE CC URICASE II LEVELS INCREASE FROM 11 TO AROUND 25 DAYS AFTER CC INOCULATION, THEN FALL SLIGHTLY. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U72663; AAB97726.1; -. DR EMBL; S75621; AAB33324.2; -. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Nodulation; Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 306 308 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 81 82 LS -> S (IN REF. 2). FT CONFLICT 140 140 V -> L (IN REF. 2). FT CONFLICT 144 144 G -> C (IN REF. 2). FT CONFLICT 171 171 N -> D (IN REF. 2). FT CONFLICT 228 230 PNR -> TKQ (IN REF. 2). FT CONFLICT 258 258 V -> C (IN REF. 2). FT CONFLICT 302 308 SRVWSKL -> LQLFYILL (IN REF. 2). SQ SEQUENCE 308 AA; 35127 MW; EE7F6050BD8F228C CRC64; MAQEVVEGFK FEQRHGKERV RVARVWRTPQ GRHFVVEWRV GITLFSDCVN SYLRDDNSDI VATDTMKNTV YAKAKECSDI LSVEDFAILL AKHFVSFYKK VTGAIVNIVE KPWERVIVDG QPHQHGFTLG SEKHTTEAIV QKSGSLQLTS GIEGLSVLKT TQSGFENFIR NKYTALPDTR ERILATEVTA LWRYSYESLY NLPQKPLYFT DKYLEVKKVL ADTFFGPPNR GVYSPSVQNT LYLMAKATLN RFPDIAYVHL KMPNLHFLPV NISSKDGPIV KFEDDVYLPT DEPHGSIEAS LSRVWSKL // ID URIC_PICJA STANDARD; PRT; 303 AA. AC P78609; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). OS Pichia jadinii (Yeast) (Candida utilis). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4903; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=IFO 0988; RX MEDLINE=97137527; PubMed=8982864; RA Koyama Y., Ichikawa T., Nakano E.; RT "Cloning, sequence analysis, and expression in Escherichia coli of the RT gene encoding the Candida utilis urate oxidase (uricase)."; RL J. Biochem. 120:969-973(1996). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D32043; BAA06804.1; -. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT ACT_SITE 168 168 PARTICIPATE IN ENZYME ACTIVITY. FT SITE 301 303 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 303 AA; 34195 MW; 0A491A4E6A39EDBF CRC64; MSTTLSSSTY GKDNVKFLKV KKDPQNPKKQ EVMEATVTCL LEGGFDTSYT EADNSSIVPT DTVKNTILVL AKTTEIWPIE RFAAKLATHF VEKYSHVSGV SVKIVQDRWV KYAVDGKPHD HSFIHEGGEK RITDLYYKRS GDYKLSSAIK DLTVLKSTGS MFYGYNKCDF TTLQPTTDRI LSTDVDATWV WDNKKIGSVY DIAKAADKGI FDNVYNQARE ITLTTFALEN SPSVQATMFN MATQILEKAC SVYSVSYALP NKHYFLIDLK WKGLENDNEL FYPSPHPNGL IKCTVVRKEK TKL // ID URIC_PIG STANDARD; PRT; 303 AA. AC P16164; DT 01-APR-1990 (Rel. 14, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UOX. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90083277; PubMed=2594778; RA Wu X., Lee C.C., Muzny D.M., Caskey C.T.; RT "Urate oxidase: primary structure and evolutionary implications."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989). RN [2] RP SEQUENCE OF 6-37 FROM N.A. RX MEDLINE=88145684; PubMed=3344434; RA Lee C.C., Wu X., Gibbs R.A., Cook R.G., Muzny D.M., Caskey C.T.; RT "Generation of cDNA probes directed by amino acid sequence: cloning RT of urate oxidase."; RL Science 239:1288-1291(1988). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -!- DATABASE: NAME=Worthington enzyme manual; CC WWW="http://www.worthington-biochem.com/manual/U/UP.html". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27697; AAA31141.1; -. DR EMBL; M19733; AAA31140.1; -. DR PIR; C36227; C36227. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT INIT_MET 0 0 BY SIMILARITY. FT SITE 301 303 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 303 AA; 34877 MW; B940A4B4252990C9 CRC64; AHYRNDYKKN DEVEFVRTGY GKDMIKVLHI QRDGKYHSIK EVATSVQLTL SSKKDYLHGD NSDVIPTDTI KNTVNVLAKF KGIKSIETFA VTICEHFLSS FKHVIRAQVY VEEVPWKRFE KNGVKHVHAF IYTPTGTHFC EVEQIRNGPP VIHSGIKDLK VLKTTQSGFE GFIKDQFTTL PEVKDRCFAT QVYCKWRYHQ GRDVDFEATW DTVRSIVLQK FAGPYDKGEY SPSVQKTLYD IQVLTLGQVP EIEDMEISLP NIHYLNIDMS KMGLINKEEV LLPLDNPYGR ITGTVKRKLT SRL // ID URIC_RABIT STANDARD; PRT; 300 AA. AC P11645; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UOX. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89247439; PubMed=2719958; RA Motojima K., Goto S.; RT "Cloning of rabbit uricase cDNA reveals a conserved carboxy-terminal RT tripeptide in three species."; RL Biochim. Biophys. Acta 1008:116-118(1989). RN [2] RP SEQUENCE OF 1-35 FROM N.A. RX MEDLINE=91099512; PubMed=2269363; RA Motojima K., Goto S.; RT "Two rabbit uricase mRNAs and their tissue-specific expression."; RL FEBS Lett. 277:26-28(1990). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14522; CAA32664.1; -. DR EMBL; X57776; CAA40922.1; -. DR EMBL; X57777; CAA40923.1; -. DR PIR; S04332; S04332. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 298 300 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 300 AA; 34500 MW; A10019A7CDA6189F CRC64; MATTKKNEDV EFVRTGYGKD MVKVLHIQRD GKYHSIKEVA TSVQLTLSSK QDYVYGDNSD IIPTDTIKNT VHVLAKFKGI KSIEVFAMNI CEHFLSSFNH VVRVHVYVEE VPWKRLEKNG VQHVHAFIHT PTGTHFCEVE QRRSGLPVIH SGIKDLKVLK TTQSGFEGFI KDQFTTLPEV KDRCFATQVY CKWRYQHSQD VDFEATWDIV RDTVLEKFAG PYDKGEYSPS VQKTLYDIQV LTLSRVPQIE DMEISLPNIH YFNIDMSKMG LINKEEVLLP LDNPYGKITG TVKRKLSSRL // ID URIC_RAT STANDARD; PRT; 302 AA. AC P09118; DT 01-MAR-1989 (Rel. 10, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Uricase (EC 1.7.3.3) (Urate oxidase). GN UOX. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=90249502; PubMed=2338140; RA Motojima K., Goto S.; RT "Organization of rat uricase chromosomal gene differs greatly from RT that of the corresponding plant gene."; RL FEBS Lett. 264:156-158(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Liver; RX MEDLINE=89034153; PubMed=3182808; RA Motojima K., Kanaya S., Goto S.; RT "Cloning and sequence analysis of cDNA for rat liver uricase."; RL J. Biol. Chem. 263:16677-16681(1988). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=89149825; PubMed=2920046; RA Alvares K., Nemali M.R., Reddy P.G., Wang X.D., Rao M.S., Reddy J.K.; RT "The nucleotide sequence of a full length cDNA clone encoding rat RT liver urate oxidase."; RL Biochem. Biophys. Res. Commun. 158:991-995(1989). RN [4] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=88196136; PubMed=3267221; RA Ito M., Suzuki M., Takagi Y.; RT "Nucleotide sequence of cDNA and predicted amino acid sequence of rat RT liver uricase."; RL Eur. J. Biochem. 173:459-463(1988). RN [5] RP SEQUENCE FROM N.A. RX MEDLINE=91153651; PubMed=1999285; RA Wang X.D., Kawano H., Alvares K., Reddy P.G., Getto H., Rao M.S., RA Reddy J.K.; RT "Rat urate oxidase: cloning and structural analysis of the gene and RT 5'-flanking region."; RL Gene 97:223-229(1991). RN [6] RP SEQUENCE OF 10-302 FROM N.A. RC TISSUE=Liver; RX MEDLINE=89057880; PubMed=3194410; RA Reddy P.G., Nemali M.R., Reddy M.K., Reddy M.N., Yuan P.M., Yuen S., RA Laffler T.G., Shiroza T., Kuramitsu H.K., Usuda N., Chisholm R.L., RA Rao M.S., Reddy J.K.; RT "Isolation and sequence determination of a cDNA clone for rat RT peroxisomal urate oxidase: liver-specific expression in the rat."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9081-9085(1988). RN [7] RP MUTAGENESIS OF LYS-163. RX MEDLINE=92392309; PubMed=1520291; RA Ito M., Kato S., Nakmura M., Go M., Takagi Y.; RT "Identification of an amino acid residue involved in the substrate- RT binding site of rat liver uricase by site-directed mutagenesis."; RL Biochem. Biophys. Res. Commun. 187:101-107(1992). CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN IN THE C-TERMINUS CC DUE TO A FRAMESHIFT. CC -!- CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN IN THE N-TERMINUS, CC CENTRAL REGION AND C-TERMINUS DUE TO FRAMESHIFTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03959; AAA42318.1; ALT_FRAME. DR EMBL; X13098; CAA31490.1; -. DR EMBL; M24396; AAA42317.1; -. DR EMBL; X07497; CAA30378.1; ALT_FRAME. DR EMBL; M63593; AAA61699.1; -. DR EMBL; M63583; AAA61699.1; JOINED. DR EMBL; M63586; AAA61699.1; JOINED. DR EMBL; M63587; AAA61699.1; JOINED. DR EMBL; M63588; AAA61699.1; JOINED. DR EMBL; M63590; AAA61699.1; JOINED. DR EMBL; M63591; AAA61699.1; JOINED. DR EMBL; M63592; AAA61699.1; JOINED. DR PIR; S00496; RDRTU. DR PIR; A31261; A31261. DR PIR; A31774; A31774. DR PIR; A32267; A32267. DR PIR; S09670; S09670. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00366; URICASE; 1. KW Oxidoreductase; Peroxisome; Purine metabolism. FT INIT_MET 0 0 FT SITE 163 163 INVOLVED IN SUBSTRATE-BINDING (PROBABLE). FT SITE 300 302 MICROBODY TARGETING SIGNAL (POTENTIAL). FT MUTAGEN 163 163 K->E,I: LOSS OF ACTIVITY. FT CONFLICT 110 110 Y -> H (IN REF. 3; AAA42317). SQ SEQUENCE 302 AA; 34803 MW; 320B601457631139 CRC64; AHYHDDYGKN DEVEFVRTGY GKDMVKVLHI QRDGKYHSIK EVATSVQLTL RSKKDYLHGD NSDIIPTDTI KNTVHVLAKF KGIKSIETFA MNICEHFLSS FSHVTRAHVY VEEVPWKRFE KNGVKHVHAF IHTPTGTHFC DVEQVRNGPP IIHSGIKDLK VLKTTQSGFE GFIKDQFTTL PEVKDRCFAT QVYCKWRYQN RDVDFEATWG AVRDIVLKKF AGPYDRGEYS PSVQKTLYDI QVLTLSQLPE IEDMEISLPN IHYFNIDMSK MGLINKEEVL LPLDNPYGKI TGTVRRKLPS RL // ID URIC_SOYBN STANDARD; PRT; 309 AA. AC P04670; P34805; P93160; P93161; O04105; DT 13-AUG-1987 (Rel. 05, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase II isozyme 1 (EC 1.7.3.3) (Urate oxidase) (Nodulin 35) (N-35) DE (Nodule specific uricase). OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. PRIZE; RA Suzuki H., Verma D.P.S.; RT "Soybean nodule-specific uricase (nodulin-35) is expressed and RT assembled into a functional tetrameric holoenzyme in Escherichia RT coli."; RL Plant Physiol. 95:384-389(1991). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 245-262. RC STRAIN=CV. PRIZE; RA Nguyen T., Zelechowska M., Foster V., Bergmann H., Verma D.P.S.; RT "Primary structure of the soybean nodulin-35 gene encoding uricase II RT localized in the peroxisome of uninfected cells of nodules."; RL Proc. Natl. Acad. Sci. U.S.A. 82:5040-5044(1985). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. AKISENGOKU; TISSUE=Cotyledon, and Root nodules; RA Takane K., Tanaka K., Tajima S., Okazaki K., Kouchi H.; RT "Expression of uricase II gene (nodulin-35) in cotyledons of soybean RT plants."; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CV. AKISENGOKU; TISSUE=Root nodules; RA Takane K., Tajima S., Kouchi H.; RT "Two distinct uricase II (nodulin 35) genes are differentially RT expressed in soybean plants."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS IS A SUBUNIT OF THE NODULE SPECIFIC URICASE. CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- INDUCTION: DURING NODULATION IN LEGUME ROOTS AFTER RHIZOBIUM CC INFECTION. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63743; AAA33997.1; -. DR EMBL; M95400; AAA34019.1; -. DR EMBL; L00353; AAA33995.1; -. DR EMBL; D86929; BAA13184.1; -. DR EMBL; D86930; BAA13185.1; -. DR EMBL; AB002810; BAA19673.1; -. DR PIR; A25776; A25776. DR Mendel; 13686; GLYma;1087;1. DR Mendel; 16777; GLYma;1087;mn16777. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Nodulation; Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 307 309 MICROBODY TARGETING SIGNAL (POTENTIAL). FT VARIANT 3 3 Q -> K (IN CV. AKISENGOKU). FT VARIANT 235 235 S -> T. FT CONFLICT 60 60 D -> E (IN REF. 2). FT CONFLICT 195 195 Y -> C (IN REF. 4). SQ SEQUENCE 309 AA; 35138 MW; 6FBC2A758FBAA982 CRC64; MAQQEVVEGF KFEQRHGKER VRVARVWKTR QGQHFIVEWR VGITLFSDCV NSYLRDDNSD IVATDTMKNT VYAKAKECSD ILSAEEFAIL LAKHFVSFYQ KVTGAIVNIV EKPWERVTVD GQPHEHGFKL GSEKHTTEAI VQKSGSLQLT SGIEGLSVLK TTQSGFVNFI RDKYTALPDT RERMVATEVT ALWRYSYESL YSLPQKPLYF TEKYQEVKKV LADTFFGPPK GGVYSPSVQN TLYLMAKATL NRFPDIAYVS LKLPNLHFIP VNISNQDGPI VKFEDDVYLP TDEPHGSIQA SLSRLWSKL // ID URID_CANLI STANDARD; PRT; 301 AA. AC P34799; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Uricase II clone PCCLNUO-02 (EC 1.7.3.3) (Urate oxidase). OS Canavalia lineata. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Canavalia. OX NCBI_TaxID=28957; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Root nodules; RA Bang K.H., An C.S.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS IS A SUBUNIT OF THE NODULE SPECIFIC URICASE. CC -!- CATALYTIC ACTIVITY: URATE + O(2) + H(2)O = 5-HYDROXYISOURATE + CC H(2)O(2) (5-HYDROXYISOURATE DECOMPOSE TO FORM ALLANTOIN). CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO THE URICASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76287; CAA53905.1; -. DR InterPro; IPR002042; Uricase. DR Pfam; PF01014; Uricase; 1. DR PRINTS; PR00093; URICASE. DR ProDom; PD003367; Uricase; 1. DR PROSITE; PS00366; URICASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Nodulation; Oxidoreductase; Peroxisome; Purine metabolism. FT SITE 299 301 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 301 AA; 34035 MW; E90B96F7B5BD5294 CRC64; MAKEIVGGFK FDQRHGKERV RVARVWKTKK GGYFIVEWRV GISLLSDCVN SYVRDDNSDI VATDTMKNTV YAKAKECSEI LSVEDFAILL AKHFISFYKQ VTAAIVNIVE KPWERVSVDG QPHEHGFKLG SERHTAEAIV QKSGALQLTS GIEGLSLLKT TKSGFEGFIR DKYTALPETH ERMLATEVTA LWRYSYESLY SIPQKPLYFT DKYLEVKKVL ADTFFGPPNV GVYSPSVQNT LYLMAKAHSS IQLKMPNIHF LPVNISNKDG PIVKFDDDVY FPTDEPHGSI QASLSRLWSK L // ID YKB4_CAEEL STANDARD; PRT; 255 AA. AC P41942; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Hypothetical 28.1 kDa protein B0272.4 in chromosome III. GN B0272.4. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Sulston J.; RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE ENOYL-COA HYDRATASE/ISOMERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z46240; CAA86314.1; -. DR HSSP; P14604; 2DUB. DR WormPep; B0272.4; CE00853. DR InterPro; IPR001753; Enoyl_CoA_hydrtse. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Hypothetical protein; Isomerase; Peroxisome. FT SITE 253 255 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 255 AA; 28107 MW; 3A4B2FB9ACF97337 CRC64; MTSGLILTER KNNVLWVTLN RPKKFNALTR QMFLDLCTVF NDAADDDDIA FVVFTGGKGK YYCAGSDFSP AELSTLTDIQ EHGYKLFVDI LIAFPKPIIA LVNGHAVGVS VTMLGVMDAV IAIDTATFAT PFADIGVCPE ACSSYTLPRI MGHQKAAALM MFSEKFTAHE AHIAGLVTQI LPAATFEKDA KKIIDRYSKL SPITMKVAKE LMRTTQIKDE LLTVNRKEQV HLNGMFSHED TIARLTAKFV KPSKI // ID ACE1_SOYBN STANDARD; PRT; 558 AA. AC P45456; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Isocitrate lyase 1 (EC 4.1.3.1) (Isocitrase 1) (Isocitratase 1) DE (ICL 1) (Fragment). GN ICL1. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MAPLE ARROW; TISSUE=Cotyledon; RA Guex N., Henry H., Widmer F.; RL Submitted (XXX-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L02329; AAA33976.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome; KW Multigene family. FT NON_TER 1 1 FT ACT_SITE 195 195 BY SIMILARITY. FT SITE 556 558 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 558 AA; 62845 MW; 99B5CA5EA24F5DDB CRC64; EAEVAEVQAW WNSERFRLTK RPYTARDVVS LRGNLRQTYA SNEMAKKLWR LLKNHQANGT ASRTFGALDP VQVTQMAKHL DTIYVSGWQC SATHTTSNEP GPDLADYPYD TVPNKVEHLF FAQQYHDRKQ KEERMRMSRE ERARTPYVDY LRPIIADGDT GFGGTTATVK LCKLFVERGA AGIHIEDQSS VTKKCGHMAG KVLVAISEHI NRLVAARLQF DVMGVETVLV ARTDAEAANL IQSNIDTRDH QFILGVTNPN LKGKSLATLM QQGMAAGKNG AELQALEDEW LSKAQLKTLS EAVVEAIERQ NNIGEEEKRR KLNEWMHHSS YERCLSNEEG REIAEKLGVR NLFWDWDLPR TREGFYRFKG SVTASVVRGC AFSPHADVIW METASPNVVE CTEFSEGVRS KHPQMMLGYN LSPSFNWDAS GMSDEQMKDF IPKIAKLGYV WQFITVGGLH SNALITSTFA RDFANRGMLA YVERIQREER NNGVDTLAHQ KWAGANYYDR YLKTVQGGVA STAAMGKGVT EEQFKESWTR SGAVNIDRGS IVVAKARM // ID ACE2_SOYBN STANDARD; PRT; 557 AA. AC P45457; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Isocitrate lyase 2 (EC 4.1.3.1) (Isocitrase 2) (Isocitratase 2) DE (ICL 2) (Fragment). GN ICL2. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MAPLE ARROW; TISSUE=Cotyledon; RA Guex N., Henry H., Widmer F.; RL Submitted (XXX-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L02330; AAA33977.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome; KW Multigene family. FT NON_TER 1 1 FT ACT_SITE 195 195 BY SIMILARITY. FT SITE 555 557 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 557 AA; 62840 MW; 486D5CE420B7AD95 CRC64; EAEVAEVQAW WNSERFRLTK RPYTARDVVS LRGNLRQTYA SNEMAKKLWC LLKNHQANGT ASRTFGALDP VQVTQMAKHL DTIYVSGWQC SATHTTSNEP GPDLADYPYD TVPNKVEHLF FAQQYHDRKQ REERMRMSRE ERARTPYVDY LRPIIADGDT GFGGTTATVK LCKLFVERGA AGIHIEDQSS VTKKCGHMAG KVLVAISEHI NRLVAARLQF DVMGVETVLV ARTDAEAANL IQSNIDTRDH QFILGVTNPN LKGKSLATLM QQGMAAGKSG AELQALEDEW LSKAQLKTLS EAVVEAIERQ NIGEEEKRRK LNEWMHHSSY ERCLSNEEGR EIAEKLGVRN LFWDWDLPRT REGFYRFKGS VIASVVRGWA FSPHADVIWM ETASPNVIEC TQFSEGVRSK HPQMMLGYNL SPSFNWDASG MSDEQMRDFI PKIAKLGYVW QFITVGGLHS NALITSTFAR DFANRGMLAY VERIQREERN NGVDTLAHQK WAGANYYDRY LKTVQGGVAS TAAMGKGVTE EQFKESWTRP GAVEIDRGSI VVAKARM // ID ACEA_BRANA STANDARD; PRT; 576 AA. AC P25248; O04910; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92393389; PubMed=2535504; RA Comai L., Dietrich R.A., Maslyar D.J., Baden C.S., Harada J.J.; RT "Coordinate expression of transcriptionally regulated isocitrate RT lyase and malate synthase genes in Brassica napus L."; RL Plant Cell 1:293-300(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93241152; PubMed=8479425; RA Zhang J.Z., Gomez-Pedrozo M., Baden C.S., Harada J.J.; RT "Two classes of isocitrate lyase genes are expressed during late RT embryogeny and postgermination in Brassica napus L."; RL Mol. Gen. Genet. 238:177-184(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. GLOBAL; TISSUE=Cotyledon; RA Olesen C., Thomsen K.K., Svendsen I., Brandt A.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MAXIMALLY DURING POSTGERMINATIVE CC GROWTH. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08482; AAA32992.1; -. DR EMBL; Y13356; CAA73792.1; -. DR PIR; JQ1105; WZRPI. DR HSSP; P16117; 1PRA. DR Mendel; 16518; Brana;1029;16518. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 213 213 PROBABLE. FT SITE 574 576 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 75 75 A -> V (IN REF. 3). FT CONFLICT 177 177 D -> G (IN REF. 3). FT CONFLICT 256 256 A -> P (IN REF. 3). FT CONFLICT 278 278 S -> N (IN REF. 3). FT CONFLICT 340 340 N -> T (IN REF. 3). FT CONFLICT 344 344 N -> I (IN REF. 3). SQ SEQUENCE 576 AA; 64325 MW; 81A87701A4ACC350 CRC64; MAASFSVPSM IMEEEGRFEA EVAEVQTWWS SERFKLTRRP YTARDVVALR GHLKQGYASN EMAKKLWRTL KSHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER AKTPFVDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGTETVLVAR TDAVAATLIQ SNIDSRDHQF ILGVTNPSLR GKSLSSLLAE GMAVGNNGPA LQAIEDQWLS SARLMTFSDA VVEALKRMNL SENEKSRRVN EWLNHARYEN CLSNEQGREL AAKLGVTDLF WDWDLPRTRE GFYRFQGSVT AAVVRGWAFA QIADLIWMET ASPDLNECTQ FAEGVKSKTP EVMLAYNLSP SFNWDASGMT DQQMMEFIPR IARLGYCWQF ITLAGFHADA LVVDTFAKDY ARRGMLAYVE RIQREERSNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA AMGKGVTEEQ FKETWTRPGA AGMGEGTSLV VAKSRM // ID ACEA_COPCI STANDARD; PRT; 537 AA. AC O13439; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ACU-7. OS Coprinus cinereus (Inky cap fungus). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; Coprinaceae; Coprinus. OX NCBI_TaxID=5346; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=JV6; RX MEDLINE=97183660; PubMed=9031626; RA Chaure P.T., Casselton L.A., Connerton I.F.; RT "Molecular analysis of the isocitrate lyase gene (acu-7) of the RT mushroom Coprinus cinereus."; RL Gene 184:185-187(1997). CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98860; CAA67367.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 203 203 BY SIMILARITY. FT SITE 535 537 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 537 AA; 59358 MW; EEAB953191CDFA82 CRC64; MSSERAQFAS EVAEVERWWK SPRFARVNRP YTAADVVSKR GTIKINYPSD VQGKKLWKLL SEHAKNGTPS HTYGALDPVQ VTKMAKYLET VYVSGWQSSS TASSSNEPGP DLADYPSNTV PNKVEHLFMA QLFHDRKQRE ARSRMSDAEL ANTPVIDYLR PIVADADTGH GGLTAVMKLT KMFVEKGAAG IHIEDQAPGT KKCGHMAGKV LVPIQEHINR LVAIRLQYDI MGVENLVVAR TDSEAATLIT SNIDDRDHPF IQGSTNPSLP PLNNVMVEAE AQGKTGDQLQ AIEDGWIKAA NLQLFPQALA QALANEGASR STVEKLVARV SRLSWSQAVA VAQKEFGLKQ VPYWNWDAPR TREGYYRYQG GTECAIHRAN AFAPYADLLW METKKPILAQ AKEFAAGVHA VHPGQWLAYN LSPSFNWKLL PQRQDMQAYV WELGKLGFVW QFITLAGLHS NAYISDLFAQ NFAKTGMKAY VELVQSRERE IGCDVLTHQK WSGADYADSL IKTVTGGVSS TAAMGAGVTE SQFTSKL // ID ACEA_CUCMA STANDARD; PRT; 576 AA. AC P93110; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Cotyledon; RX MEDLINE=97134001; PubMed=8979395; RA Mano S., Hayashi M., Kondo M., Nishimura M.; RT "cDNA cloning and expression of a gene for isocitrate lyase in pumpkin RT cotyledons."; RL Plant Cell Physiol. 37:941-948(1996). CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D78256; BAA11320.1; -. DR Mendel; 7775; Cucma;1029;7775. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 213 213 BY SIMILARITY. FT SITE 574 576 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 576 AA; 64358 MW; 269D93D4F13B5990 CRC64; MATSFSVPSM IMEEEGRFEA EVAEVQAWWN SERFKLTRRP YTAKDVVSLR GSLRQSYASN DLAKKLWRTL KTHQANSTAS RTFGALDPVQ VTMMAKHLDS IYVSGWQCSS THTSTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER AKTPYVDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGVETVLVAR TDAVAATLIQ TNVDSRDHQF ILGATNPNLR GKSLAGVLAE AMAAGKTGAE LQALEDQWIS MAQLKTFSEC VTDAIMNSNG TESEKRRKLD EWMNHSSYEK CISNEQGREI AEKLGLKNLF WDWDLPRTRE GFYRFKGSVM AAIVRGWAFA PHADLIWMET SSPDLVECTT FAKGVKSVHP EIMLAYNLSP SFNWDASGMS DKQMEEFIPT IARLGFCWQF ITLAGFHADA LVIDTFARDY ARRGMLAYVE RIQREERNNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA AMGKGVTEEQ FKESWTRAGA GNLGEEGSVV VAKSRM // ID ACEA_CUCSA STANDARD; PRT; 576 AA. AC P49296; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). OS Cucumis sativus (Cucumber). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucumis. OX NCBI_TaxID=3659; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MASTERPIECE; TISSUE=Leaf; RX MEDLINE=95201243; PubMed=7894014; RA Reynolds S.J., Smith S.M.; RT "The isocitrate lyase gene of cucumber: isolation, characterisation RT and expression in cotyledons following seed germination."; RL Plant Mol. Biol. 27:487-497(1995). CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z35499; CAA84632.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 213 213 PROBABLE. FT SITE 574 576 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 576 AA; 64611 MW; 717D30B83CD81D6C CRC64; MAASFSVPSM IMEEEGRFEA EVAEVQAWWN SERFKLTRRP YTAKDVVSLR GSLRQSYASN DLAKKLWRTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER AKTPYIDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGVETILVAR TDAVAATLIQ TNVDKRDHQF ILGATNPNLR GKSLAGALAE AMAAGKTGAE LQALEDQWIS MAQLKTFSEC VTDAIMNTNA TENEKRRKLD EWMNHSSYEK CISNEQGREI AEKLGLKNLF WDWDLPRTRE GFYRFKGSVM AAIVRGWAFA PHADLIWMET SSPDLVECTT FAKGMKSIHP ETMLAYNLSP SFNWDASGMS DKQMEEFIPR IARLGFCWQF ITLAGFHADA LVVDTFARDY ARRGMLAYVE RIQREERNNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA AMGKGVTEEQ FKESWTREGA VNLGEEGNVV VAKSRM // ID ACEA_DENCR STANDARD; PRT; 574 AA. AC Q9SE26; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ICL. OS Dendrobium crumenatum (Tropical pigeon orchid). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Orchidaceae; OC Epidendroideae; higher Epidendroideae; Dendrobieae; Dendrobiinae; OC Dendrobium. OX NCBI_TaxID=51096; RN [1] RP SEQUENCE FROM N.A. RA Vellupillai M., Goh C.-J., Swarup S.; RT "Sequence analysis of DcrIcl, an isocitrate lyase gene from the RT tropical orchid, Dendrobium crumenatum."; RL (In) Plant Gene Register PGR99-178. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- DEVELOPMENTAL STAGE: EXPRESSED MAXIMALLY DURING POSTGERMINATIVE CC GROWTH. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF193815; AAF04598.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 212 212 PROBABLE. FT SITE 572 574 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 574 AA; 63993 MW; 0B568ADE3248DE2E CRC64; MASSSVPPMI TEEEARFEAE VSAVESWWRT DRFRLTRRPY SARDVVSLRG TLHHSYASDQ MAKKLWRTLK SHQSAGTASR TFGALDPVQV TMMAKHLDTI YVSGWQCSST HTATNEPGPD LADYPYNTVP NKVEHLFFAQ LYHDRKQHEA RVSMTREQRA KTPYVDYLRP IIADGDTGFG GATATVKLCK LFVERGAAGV HIEDQSSVTK KCGHMAGKVL VAVSEHINRL VAARLQFDVM GVETVLVART DAVAATLIQS NVDLRDHQFI LGATNPDFKR RSLAAVLSAA MAAGKTGAVL QAIEDDWLSR AGLMTFSDAV INGINRQNLP EYEKQRRLNE WAAATEYSKC VSNEQGREIA ERLGAGEIFW DWDIARTREG FYRFRGSVEA AVVRGRAFAP HADLIWMETS SPDLVECGKF AQGMKASHPE IMLAYNLSPS FNWDAAGMTD EEMRDFIPRI AKMGFCWQFI TLGGFHADAL VTDTFAREFA KQGMLAYVER IQREERNNGV DTLAHQKWSG ANYYDRYLKT VQGGISSTAA MGKGVTEEQF KEESRTGTRG LDRGGITVNA KSRL // ID ACEA_GOSHI STANDARD; PRT; 576 AA. AC P17069; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 01-DEC-1992 (Rel. 24, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). OS Gossypium hirsutum (Upland cotton). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Malvales; Malvaceae; Gossypium. OX NCBI_TaxID=3635; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. DELTAPINE 62; TISSUE=Cotyledon; RX MEDLINE=90304228; PubMed=2194576; RA Turley R.B., Choe S.M., Trelease R.N.; RT "Characterization of a cDNA clone encoding the complete amino acid RT sequence of cotton isocitrate lyase."; RL Biochim. Biophys. Acta 1049:223-226(1990). CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52136; CAA36381.1; -. DR PIR; S10771; WZCNIU. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 213 213 PROBABLE. FT SITE 574 576 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 576 AA; 64733 MW; 84D211AA3DCE8700 CRC64; MAASFSVPSM IMEEEGRFET EVAEVQAWWN SERFKLTRRP YSARDVVALR GSLKQSYGSN EMAKKLWTTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDS IYVSGWQCSS THTTTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER ARTPYVDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGVETVLVAR TDAVAATLIQ TNVDTRDHQF ILGATNPNLR GKSLANMLAE GMAAGKNGPQ LQAIEDNWLA IAQLKTFSEC VMDAIKSMNI TEDEKRRRMN EWMNHSSYDK CLSNEQAREI AERLGLQNLF WDWDLPRTRE GFYRFRGSVM AAIVRGWAFA PHADLIWMET SSPDMVECTR FAEGVKSMHP EIMLAYNLSP SFNWDASGMT DEHMRDFIPR IAKLGFCWQF ITLAGFHADA LVTDTFARDF ARRGMLAYVE KIQREERNNG VDTLAHQKWS GANFYDRYLK TVQGGISSTA AMGKGVTEEQ FKETWTRPGA GNIGSEGNLV VAKARM // ID ACEA_LYCES STANDARD; PRT; 575 AA. AC P49297; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. UC82B; TISSUE=Leaf; RX MEDLINE=95357440; PubMed=7630969; RA Janssen B.J.; RT "A cDNA clone for isocitrate lyase from tomato."; RL Plant Physiol. 108:1339-1339(1995). CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U18678; AAA82738.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 213 213 PROBABLE. FT SITE 573 575 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 575 AA; 64720 MW; F398FA96C7110B4E CRC64; MAASYSVPSM IMEEERRFEA EVAEVQAWWN TERFRLTKRA YSARDVVALR GTMRQSYASN ELAQKLWRTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMCREER ARTPFIDYLK PIIADGDTGF GGATATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV MGTETVLVAR TDAVAATLIQ TNVDTRDHQF ILGASNPNLK GKGLATHLSE AMAAGKTGPE LQAIEDNWLG MAELKTFSQC VTDAIKKMNL AEYEKQRKLN EWMNHSSYEK CLSHEQAREV AERLGLPNLF WDWDLPRTRE GFYRFQGSVE AAIVRGWAFA EYCDLVWMET SSPDMVECTK FSQGVKTLRP ELMLAYNLSP SFNWDASGMN DNQMMDFIPR IAKLGYCWQF ITLAGFHADA LIVDTFAKDF ARRGMLAYVE KIQREERSNG VDTLAHQKWS GANYYDRVLR TVQGGITSTA AMGKGVTEEQ FEEKWTRTGA TNLGDGSVVI AKARM // ID ACEA_PINTA STANDARD; PRT; 580 AA. AC Q43097; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ICL 8. OS Pinus taeda (Loblolly pine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=3352; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97238466; PubMed=9132051; RA Mullen R.T., Gifford D.J.; RT "Regulation of two loblolly pine (Pinus taeda L.) isocitrate lyase RT genes in megagametophytes of mature and stratified seeds and during RT postgerminative growth."; RL Plant Mol. Biol. 33:593-604(1997). CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U39807; AAC49687.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 215 215 PROBABLE. FT SITE 578 580 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 580 AA; 64676 MW; E85785DAE970D697 CRC64; MAIYSAQAPN SILEEEARFE AEVSETQAWW NSTDLFRLTR RPYTARDVVR LRGSMRQSYA SNEMAKKLWR TLKTHQANKT ASRTFGALDP VQVSMMAKYL DSIYVSGWQC SSTHTTTNEP GPDLADYPYD TVPNKVEHLF FAQQFHDRKQ KEARMSMTRE ERSKTPYIDY LKPIIADGDT GFGGATATVK LCKLFVERGA AGVHIEDQAS VTKKCGHMAG KVLVSVGEHV NRMVAARLQF DIMGVETLLV ARTDAVAATL IQTNVDARDH QFILGATNPN LKGKPLADVL ARAMASGKSG ADLQAVEDEW MAMADLKLFS DCVVDGIKAL NVSEQEKGRR LGEWMQQTGG NTGNVLSYYQ AKELAEKLGI SNLFWDWDLP RTREGFYRFQ GSVKAAIVRG WAFGPHADII WMETSSPDMV ECRDFALGVK SKHPEIMLAY NLSPSFNWDA SRMTDEQMKN FIPEIARLGY CWQFITLAGF HADALVIDTF AKDFAQRGML AYVEKIQRQE MMNGVDTLAH QKWSGANYYD QLLKTVQGGI SATAAMAKGV TEDQFEETQS STLALESNIG AGTVLAKSRM // ID ACEA_RICCO STANDARD; PRT; 576 AA. AC P15479; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-DEC-1992 (Rel. 24, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Malpighiales; Euphorbiaceae; Ricinus. OX NCBI_TaxID=3988; RN [1] RP SEQUENCE FROM N.A. RA Beeching J.R., Northcote D.H.; RT "Nucleic acid (cDNA) and amino acid sequences of isocitrate lyase from RT castor bean."; RL Plant Mol. Biol. 8:471-475(1987). CC -!- FUNCTION: INVOLVED IN STORAGE LIPID MOBILIZATION DURING THE GROWTH CC OF HIGHER PLANT SEEDLING. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17145; AAA53378.1; -. DR PIR; S06274; WZCSI. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 213 213 PROBABLE. FT SITE 574 576 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 576 AA; 64751 MW; 8177A7679050579B CRC64; MAASFSGPSM IMEEEGRFEA EVAEVQAWWN SERFKLTRRP YTARDVVALR GNLKQSYASN ELAKKLWRTL KTHQANGTAS RTFGALDPVQ VTMMAKHLDS IYVSGWQCSS THTTTNEPGP DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER ARTPYVDYLK PIIADGDTGF GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAISEHINR LVAARLQFDV MGVETLLVAR TDAEAANLIQ SNVDTRDHQF ILGVTNPNLR GKSLATLLAT GMANGKTGAE LQATEDNWLA MAQLKTFPEC VMDAIKNMNA GEDEKRRRMN EWMNHTSYDK CLSYEQGREI ADRMGLKNLF WDWDLPRTRE GFYRFKGSVM AAVVRGRAFA PHADIIWMET AKPDFAECTA FAEGVKSMHP EIMLAYNLSP SFNWDASGMT DEQMRDFIPR IARLGFCWQF ITLGGFHADA LVIDTFAKDY ARRGMLAYVE RIQREERKNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA AMGKGVTEEQ FKETWTRPGA MEMGSAGSEV VAKARM // ID ACEA_YARLI STANDARD; PRT; 541 AA. AC P41555; DT 01-NOV-1995 (Rel. 32, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Isocitrate lyase (EC 4.1.3.1) (Isocitrase) (Isocitratase) (ICL). GN ICL1. OS Yarrowia lipolytica (Candida lipolytica). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=4952; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B204-12C; RX MEDLINE=94067025; PubMed=8246896; RA Barth G., Scheuber T.; RT "Cloning of the isocitrate lyase gene (ICL1) from Yarrowia lipolytica RT and characterization of the deduced protein."; RL Mol. Gen. Genet. 241:422-430(1993). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RC STRAIN=B204-12C; RA Juretzek T.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE. CC -!- PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI). CC -!- SUBUNIT: HOMOTETRAMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X72848; CAA51362.1; -. DR InterPro; IPR000918; Isocit_lyase. DR Pfam; PF00463; ICL; 1. DR ProDom; PD001857; Isocit_lyase; 1. DR PROSITE; PS00161; ISOCITRATE_LYASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT ACT_SITE 204 204 BY SIMILARITY. FT SITE 539 541 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 541 AA; 60436 MW; 52C5717BEBE65CEA CRC64; MSEQQRFNNE VEEIKKWWSS PRWKHTKRVY SPEDIASRRG TIKVPQASSQ QADKLFKLLQ EHEKNHTASF TYASLDPVQV TQMAKYLDSI YVSGWQCSST ASTSNESSPD LGGYPMDTVP NKVEHLWFAQ LFHERKQNEE RLSLPESEPI QAPRARVDYL RPIIADAETG HGGLTAVVKL TKMFIERGAA GIHIEDQAPG TKKCGHMAGK VLVPIQEHIN RLIAIRASAD IFALNLLAIA RTDSEAATLI TSSIDYRDHY FIAGATNKDA GHLVDVMVAA EARGQAGAPL QAVEDEWNRK AGVKLFHEAF ADEVNDGSYS NKAELIAEFN KKVTPLSNTP DIEDRYLAAR LLGKDIYFNW EAARVREGYY RYQGGTQCAV NRGYSYAPYA DLIWMESKLP DYAQAKEFAE GVKNAVPHQW LAYNLSPSFN WTTAMSPEDQ ETYISRLAKL GYVWQFITLA GLHTNALISD KSCKAYSERG MKAYGGEIQQ PEIDQGCEVV KHQKWSGAEY IDGILRMVTG GITSTAAMGA GVTEDQFKSK L // ID MASY_BRANA STANDARD; PRT; 561 AA. AC P13244; O04911; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Brassica. OX NCBI_TaxID=3708; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89123375; PubMed=2914930; RA Comai L., Baden C.S., Harada J.J.; RT "Deduced sequence of a malate synthase polypeptide encoded by a RT subclass of the gene family."; RL J. Biol. Chem. 264:2778-2782(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. GLOBAL; TISSUE=Cotyledon; RA Olesen C., Thomsen K.K., Svendsen I., Brandt A.B.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04468; AAA32996.1; -. DR EMBL; Y13357; CAA73793.1; -. DR PIR; A31428; SYRPMA. DR Mendel; 16789; BRAna;Mas1;mn16789. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 559 561 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 29 29 Q -> L (IN REF. 2). FT CONFLICT 163 163 K -> I (IN REF. 2). FT CONFLICT 172 172 A -> V (IN REF. 2). FT CONFLICT 175 175 F -> W (IN REF. 2). SQ SEQUENCE 561 AA; 63728 MW; 215A1027CD991AA3 CRC64; MELETSVYRP NVAVYDSPDG VEVRGRYDQV FAKILTRDAL GFVAELQREF RGHVRYAMEC RREVKRRYNS GAVPGFDPST KFIRDGEWVC ASVPPAVADR RVEITGPVER KMIINALNSG AKVFMADFED ALSPSWENLM RGQVNLKDAV DGSITFNDKA RNKVYKLNDQ VAKLFVRPRG WHLPEAHILI DGEPATGCLV DFGLYFFHNY AKFRQTQGSG FGPFFYLPKM EHSREAKIWN SVFERAEKMA GIERGSIRAT VLIETLPAVF QMNEILYELR DHSVGLNCGR WDYIFSYVKT FQAHPDRLLP DRVLVGMGQH FMRSYSDLLI RTCHKRGVHA MGGMAAQIPI RDDPKANEMA LDLVKKDKLR EVRAGHDGTW AAHPGLIPIC MDAFSHMGNN PNQIKSMKRD DASAITEEDL LQIPRGVRTL EGLRLNTRVG IQYLAAWLTG SGSVPLYNLM EDAATAEISR VQNWQWIRYG VELDGDGLGV RVSKELFGRV VEEEMERIEK EVGKDKFKRG MYKEACKMFT KQCTAAELDD FLTLAVYDHI VAHYPINASR L // ID MASY_CUCMA STANDARD; PRT; 566 AA. AC P24571; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 83-91; 197-206 AND 417-426. RC STRAIN=CV. KUROKAWA AMAKURI NANKIN; TISSUE=Etiolated cotyledon; RX MEDLINE=91224123; PubMed=1709098; RA Mori H., Takeda-Yoshikawa Y., Hara-Nishimura I., Nishimura M.; RT "Pumpkin malate synthase. Cloning and sequencing of the cDNA and RT northern blot analysis."; RL Eur. J. Biochem. 197:331-336(1991). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56948; CAA40262.1; -. DR PIR; S15387; S15387. DR PIR; S14601; S14601. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 564 566 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 566 AA; 64635 MW; B77F77D1D593834A CRC64; MGSLGMYSES AVRKKSSRGY DVPEGVDIRG RYDEEFARIL NKEALLFVAD LQRTFRNHIR YSMECRREAK RRYNEGAVPG FDPATKYIRE SEWTCASVPP AVADRRVEIT GPVERKMIIN ALNSGAKVFM ADFEDALSPN WENLMRGQIN LKDAVDGTIS FHDKARNKVY KLNDQTAKLF VRPRGWHFAE AHIFIDGEPA TGCLVDFGLY FFHNHANFRR SQGQGSGPFF YLPKMEHSRE AKIWNSVFER AEKMAGIERG SIRATVLIET LPAVFQMDEI LYELRDHSVG LNCGRWDYIF SYVKTFQAHL DRLLPDRVQV GMAQHFMRSY SDLLIRTCHT VVCHVGGMAA QIPIRDDPKA NEMALELVRK DKLREAKAGH DGTWAAHPGL IPACMEVFTN SMGNAPNQIR SARRDDAANL TEDDLLQQPR GVRTLEGLRL NTRVGIQYLA AWLTGTGSVP LYNLMEDAAT AEISRVQNWQ WLKYGVELDG DGLGVRVNKE LFARVVEEEM ERIEREVGKE KFRKGMYKEA CKMFTRQCTA PTLDDFLTLD AYNHIVIHHP RELSRL // ID MASY_CUCSA STANDARD; PRT; 568 AA. AC P08216; DT 01-AUG-1988 (Rel. 08, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). OS Cucumis sativus (Cucumber). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucumis. OX NCBI_TaxID=3659; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. LONG GREEN RIDGE; RX MEDLINE=91370851; PubMed=2491683; RA Graham I.A., Smith L.M., Brown J.W.S., Leaver C.J., Smith S.M.; RT "The malate synthase gene of cucumber."; RL Plant Mol. Biol. 13:673-684(1989). RN [2] RP SEQUENCE OF 475-568 FROM N.A. RA Smith S.M., Leaver C.J.; RT "Glyoxysomal malate synthase of cucumber: molecular cloning of a cDNA RT and regulation of enzyme synthesis during germination."; RL Plant Physiol. 81:762-767(1986). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15425; CAA33465.1; -. DR EMBL; M16219; AAA33123.1; -. DR PIR; S07550; SYKVMA. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 566 568 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 475 475 I -> G (IN REF. 2). SQ SEQUENCE 568 AA; 64961 MW; 0C25AB66288ECAA4 CRC64; MGSLGMYSES GLTKKGSSRG YDVPEGVDIR GRYDEEFAKI LNKEALLFIA DLQRTFRNHI KYSMECRREA KRRYNEGGLP GFDPATKYIR DSEWTCAPVP PAVADRRVEI TGPVERKMII NALNSGAKVF MADFEDALSP NWENLMRGQI NLKDAVDGTI SFHDRVRNRV YKLNDRTAKL FVRPRGWHLP EAHIFIDGEP ATGCLVDFGL YFFHNHANFR RSQGQGYGPF FYLPKMEHSR EAKIWNSVFE RAEKMAGIER GSIRATVLIE TLPAVFQMNE ILYELRDHSV GLNCGRWDYI FSYVKTFQAH PDRLLPDRVL VGMTQHFMRS YSDLLIRTCH RRGVHAMGGM AAQIPIRDDP KANEVALELV RKDKLREVKA GHDGTWAAHP GLIPACMEVF TNNMGNAPNQ IRSMRRDDAA NLTEEDLLQQ PRGVRTMEGL RLNTRVGIQY LAAWLTGAGS VPLYNLAEDA ATAEISRVQN WQWLKYGVEL DGDGLGVRVN KELFGRVVEE EMERIEREVG KERFKKGMYK EACKMFTRQC TAPNLDDFLT LDAYNYIVIH HPRELSKL // ID MASY_EMENI STANDARD; PRT; 528 AA. AC P28344; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). GN ACUE. OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=5072; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91375430; PubMed=1832736; RA Sandeman R.A., Hynes M.J., Fincham J.R.S., Connerton I.F.; RT "Molecular organisation of the malate synthase genes of Aspergillus RT nidulans and Neurospora crassa."; RL Mol. Gen. Genet. 228:445-452(1991). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56671; CAA39993.1; -. DR PIR; S17773; S17773. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 526 528 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 528 AA; 59480 MW; 044B3239E1D3EB2E CRC64; MSQVDAQLKD VAILGSVSNE ARKILTKEAC AFLAILHRTF NPTRKALLQR RVDRQAEIDK GHLPDFLPET KHIRDDPSWK GAPPAPGLVD RRVEITGPTD RKMVVNALNS DVAPTWDNMI NGQINLYDAI RRQVDFKQGQ KEYKLRTDRT LPTLIARARG WHLDEKHFTV DGEPISGSLF DFGLYFFHNA KELVARGFGP YFYLPKMESH LEARLWNDVF NLAQDYIGMP RGTIRGTVLI ETITAAFEME EIIYELRDHS SGLNCGRWDY IFSFIKKFRQ HPNFVLPDRS DVTMTVPFMD AYVKLLIKTC HKRGVHAMGG MAAQIPIKDN AEANDKAMEG VRADKLREVR AGHDGTWVAH PALASIASEV FNKYMPTPNQ MHVRREDVNI TANDLLNTNV PGKITEDGIR KNLNIGLSYM EGWLRGVGCI PINYLMEDAA TAEVSRSQLW QWARHGVTTS EGKKVDKAYA LRLLKEQADA LAAKGPKGNK FQLAGRYFSG QVTGEDYADF LTSLLYNEIS SPGTASKL // ID MASY_GOSHI STANDARD; PRT; 567 AA. AC P17432; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). OS Gossypium hirsutum (Upland cotton). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Malvales; Malvaceae; Gossypium. OX NCBI_TaxID=3635; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seed; RX MEDLINE=90301492; PubMed=2362818; RA Turley R.B., Choe S.M., Ni W., Trelease R.N.; RT "Nucleotide sequence of cottonseed malate synthase."; RL Nucleic Acids Res. 18:3643-3643(1990). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52305; CAA36546.1; -. DR PIR; S12735; SYCNMU. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 565 567 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 567 AA; 64668 MW; AC69D3BE20C91204 CRC64; MIGLGSYGYT APSSKKINAY DVPQGVDIRG RFDEEFAKIL TKDALQFVAD LQREFRNHIK YAMECRKEAK RRYNEGALPG FDPATRYIRE GKWTCVPFPP AVADRRVEIT GPVERKMIIN ALNSGAKVFM ADFEDALSPS WENLMRGQIN LKDAVEGTIT FNDKARNRVY KLNNEIAKLF VRPRGWHLPE AHIFIDGEPA TGCLVDFGLY FYHNYATFRN TQGQGFGPFF YLPKMENSRE AKIWNSVFEK AEKMAGIEKG SIRATVLIET LPAVFQMDEI FYELRDHSVG LNCGRWDYIF SYVKTFQGHP DRLLPDRGQV GMTQHFMRSY SDLLIRTCHR RGVHAMGGMA AQIPIRDDPT ANEAAFELVR KDKQREVKAG HDGTWAAHPG LIKTCMEVFT NNMGNTPNQI ETVKRDYASN LTEDDLLQRP RGVRTMEGLR LNTRVGIQYL AAWLTGSGSV PLYNLMEDAA TAEISRVQIW QWLKYGVELD GDGLGVRVNH VFGRVVEEEM ARIEREVGKE KFKKGMYKEA CKIFTRQCTA STLDDFLTLD AYNYIVIHHP KDVSSKL // ID MASY_MAIZE STANDARD; PRT; 559 AA. AC P49081; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). GN LIP. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACC clade; OC Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. TX5855; TISSUE=Scutellum; RA Paek N.C., Taylor B.H., Smith J.D.; RT "Nucleotide sequence of malate synthase cDNA in maize."; RL (In) Plant Gene Register PGR95-015. CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L35914; AAB04118.1; -. DR MaizeDB; 100137; -. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 557 559 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 559 AA; 61636 MW; BC639B38D57C530B CRC64; MAASTAAPCY DAPEGVDVRG RYDREFAGIL TRDALDFVAG LQREFRGAVR YAMEQRREAQ RRYDAGELPR FDPATTLVRE GDWTCASVPP AVADRTVEIT GPAEPRKMVI NALNSGAKVF MADFEDAMSP TWENLMHGQV NLRDAVAGTI SFRDAPRGRT YELNDRTAKL FVRPRGWHLP EAHILIDGEP AIGCLVDFGL YFFHNHAAFG AGQGAGFGPL CDLPKMEHSR EARIWNGVFQ RAEKAAGIEP GSIRATVLVE TLPAVFQMNE ILHELREHSA GLNCGRWDYI FSYVKTFRAH PDRLLPDRAL VGMAQHFMRS YSHLLIHTCH RRGVHAMGGM AAQIPIKDDA AANEAALELV RKDKLREVRA GHDGTWAAHP GLIPAIREVF EGHLGGRPNQ IGDAAGHEGA SVKEEDLIQP PRGARTVDGL RLNVRVGVQY LAAWLAGSGS VPLYNLMEDA ATAEISRVQN WQWLRHGAAL DAGGVEVRAT PELLARVVEE EMARVEAEVG PDRFRKGRYA EAGRIFSRQC TAPELDDFLT LDAYNLIVAH HPGASPCKL // ID MASY_NEUCR STANDARD; PRT; 542 AA. AC P28345; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). GN ACU-9. OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91375430; PubMed=1832736; RA Sandeman R.A., Hynes M.J., Fincham J.R.S., Connerton I.F.; RT "Molecular organisation of the malate synthase genes of Aspergillus RT nidulans and Neurospora crassa."; RL Mol. Gen. Genet. 228:445-452(1991). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56672; CAA39994.1; -. DR PIR; S17774; S17774. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 540 542 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 542 AA; 61434 MW; B8982206CAA64D5F CRC64; MASVETLLQG VTISGPIEEH QRKILTPQAL SFVALLHRSF NQTRKNLLER RHVRQAEIDR GVLPDFLPET KHIRENPTWK GAAPAAPPLV DRRVEMTGPT DRKMVVNALN SDVYTYMADF EDSSAPTWAN MVNGQVNLYD AIRRQIDFKQ GPKEYKLRTD RTLPTLIVRP RGWHLEEKHV TIDGEPVSGS LFDFGLYFFH NAKELVQRGF GPYFYPPKME SHLEARLWND AFNLAQDYVG IPLSTIRGTV LIETITAAFE MDEIIFELRN HTSGLNRGGW DYIFPFIKEV RRFPNFVLPD RSDVTMTVPF MEAYVKLLIK TLHRLVVHAM GMAAQIPIKD DKAANDKAME GVRADKLREA RAGHDGTWVA HPALASIALE VFNKHMPTPN QLFNRREDVK IGQQDLLNMN VPGSSTEDGI RKNLNTGLGY TEPWIRGVGC VPIKHPQEDA ATAEVSRSQL WQWVKHRVTT AEGKHVDKRY PLKLLKEADR QRLAKAPQGN KFNLAAQYFA SQVTGEDYAD FLTCLLYNEI TSAGNSLPAS KL // ID MASY_RAPSA STANDARD; PRT; 566 AA. AC Q43827; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). GN MLS. OS Raphanus sativus (Radish). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Raphanus. OX NCBI_TaxID=3726; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. SAXA KNACKER; TISSUE=Seedling; RA Vollack K.U., Bach T.J.; RT "Overexpression of radish malate synthase in yeast."; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78852; CAA55407.1; -. DR Mendel; 147; RAPsa;Mas1;1. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 564 566 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 566 AA; 64137 MW; 807104112623FF77 CRC64; MELETSVYRP NAAVYDSPDG VEVRGRYDQV FAKILTREAL GFVAELQRDV SLGMLRYAWS AVERQNVVTT FVLSLGLTLP LSSSEIGEWV CSVCSPPAVA DRRVEITGPV ERKMIINALN SGAKVFMADF EDALSPSWEN LMKGQVNLKD AVDGTITFHD KARNKVYKLN DQVAKLFVRP RGWHLPEAHI LIDGEPAIGC LVDFGLYFFH NYSKFRQTQG SGYGPFFYLP KMEHSREAKI WNSVFERAEK MAGIERGSIR ATVLIETLPA VFQMNEILYE LRDHSVGLNC GRWDYIFSYV KTFQAHPDRL LPDRVLVGMG QHFMRSYSDL LIRTCHKRGV HAWEGMAAQI AIRDDPKAND MALDLVKKDK LRQVRAGHDG TWAAHPGLIP ICMDAFGHMG KNPNQIKSMK RDDASAITEE DLLQIPRGVR TLDGLRLNTR VGIQYLAAWL TGSGSVPLYN LTDEDAATAE ISRVQNWQWI RYGVELKRRT GLEVRVSKEL FGRVVEEEME RIEKEVGKER SLREECIRKL ARCLQSSVTA AELDDFLTLA VYDHIVAHYP INVSRL // ID MASY_RICCO STANDARD; PRT; 567 AA. AC P17815; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2). OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Malpighiales; Euphorbiaceae; Ricinus. OX NCBI_TaxID=3988; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Endosperm; RX MEDLINE=91355898; PubMed=2103467; RA Rodriguez D., Ginger R.S., Baker A., Northcote D.H.; RT "Nucleotide sequence analysis of a cDNA clone encoding malate synthase RT of castor bean (Ricinus communis) reveals homology to DAL7, a gene RT involved in allantoin degradation in Saccharomyces cerevisiae."; RL Plant Mol. Biol. 15:501-504(1990). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52806; CAA36994.1; -. DR PIR; S14677; SYCSM2. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT SITE 565 567 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 567 AA; 64262 MW; 3888DCAF87CD36E2 CRC64; MRYDTYGDSA PIKKTGAGYD VPEGVDIRGR YDGEFAKILT RDALQFVADL QREFRNRIRY AIECRKEAKS RYNAGALPGF EHPATKYIRE GEWTCAPVPP AVADRKVEIT GPVERKMIIN ALNSGAKVFM ADFEDALSPS WENLMRGQVN LRDAVNGTIS FHDKARNRVY KLNDQIAKLF VRPRGWHLPE AHILIDGEPA TGCLVDFGLY FYHNYAAFRR NQGAGYGPFF YLPKMEHSRE AKIWNCVFEK AEKMAGIERG SIRATVLIET LPAVFQMNEI LYELRDHSVG LNCGRWDYIF SYVKTFQAHP DRPLPDRVQV GMTQHFMKSY SDLLVWTCHR RGVHAMGGMA AQIPIRDDPA ANKAALELVR KDKLREVKAG HDGTWAAHPG LIPACMEVFA NNMGNTPHQI QAMKREDAAN ITEEDLIQRP RGVRTLEGLR LNTRVGIQYL AAWLTGTGSV PLYNLMEDAA TAEISRVQNW QWLKYGVELD GDGLGVKVTF DLLGRVVEDE MARIEREVGK EKFKKGMYKE ACKMFVRQCA APTLDDFLTL DAYNNIVIHY PKGSSRL // ID MASY_SOYBN STANDARD; PRT; 564 AA. AC P45458; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase, glyoxysomal (EC 4.1.3.2) (MS) (Fragment). OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MAPLE ARROW; TISSUE=Cotyledon; RX MEDLINE=96081525; PubMed=8547819; RA Guex N., Henry H., Flach J., Richter H., Widmer F.; RT "Glyoxysomal malate dehydrogenase and malate synthase from soybean RT cotyledons (Glycine max L.): enzyme association, antibody production RT and cDNA cloning."; RL Planta 197:369-375(1995). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L01629; AAC37465.1; -. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome. FT NON_TER 1 1 FT SITE 562 564 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 564 AA; 63909 MW; EE175238AEA6185A CRC64; GTYGYPTPAV KKIESYYDVP EGVDIRGRYD AEFAKILTKD ALKFVADLQR EFRNHIKYAL ECRREAKKKY NEGALPEFDP ATTYIREQEW VCAPVPPAVA DRKVEITGPV DRKMVINALN SGAKVFMADF EDALSPGWEN LMRGQVNLKD AVAGTISLHD KARNRVYKLN DQTAKLFVRP RGWHLPEAHI LIDGEPATGC LVDFGLYFYH SYSAFRRTQG AGFGPFFYLP KMEHSREAKI WNNVFEKAEK VAGIERGSIR ATVLIETLPA VFQMNEILYE LKDHSVGLNC GRWDYIFSYV KTFQAHPDRL LPDRVLVGMT QHFMKSYSDL LIRTCHRRGV HAMGGMAAQI PIKEDPVANE VALELVRKDK LREVKAGHDG TWAAHPGLIP ACMEIFNNNM GNASNQIDTV KREDGANITE QDLLQIPRGA RTMEGLRLNT RVGIQYVAAW LTGSGSVPLY NLMEDAATAE ISRVQNWQWL KYGVELNGDG LGVKVNKELF GRVVEEEMAR IEKEVGTEKF KEGMYKEACK IFTRQCTSPM LDDFLTLDAY NYIVVHHPRE TSKL // ID MASY_YEAST STANDARD; PRT; 554 AA. AC P30952; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase 1, glyoxysomal (EC 4.1.3.2). GN MLS1 OR YNL117W OR N1921. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93087177; PubMed=1454530; RA Hartig A., Simon M.M., Schuster T., Daugherty J.R., Yoo H.S., RA Cooper T.G.; RT "Differentially regulated malate synthase genes participate in carbon RT and nitrogen metabolism of S. cerevisiae."; RL Nucleic Acids Res. 20:5677-5686(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=97245296; PubMed=9090055; RA de Antoni A., D Angelo M., Dal Pero F., Sartorello F., Pandolfo D., RA Pallavicini A., Lanfranchi G., Valle G.; RT "The DNA sequence of cosmid 14-13b from chromosome XIV of RT Saccharomyces cerevisiae reveals an unusually high number of RT overlapping open reading frames."; RL Yeast 13:261-266(1997). CC -!- FUNCTION: THIS ISOZYME IS NECESSARY FOR GROWTH ON ACETATE AS SOLE CC C-SOURCE. CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBUNIT: HOMOTRIMER. CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64407; CAA45750.1; -. DR EMBL; Z69382; CAA93390.1; -. DR EMBL; Z71393; CAA95997.1; -. DR PIR; S20125; S20125. DR PIR; S26645; S26645. DR YEPD; 4704; -. DR SGD; S0005061; MLS1. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome; KW Multigene family. FT SITE 552 554 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 554 AA; 62791 MW; 98E698E86E59C480 CRC64; MVKVSLDNVK LLVDVDKEPF FKPSSTTVGD ILTKDALEFI VLLHRTFNNK RKQLLENRQV VQKKLDSGSY HLDFLPETAN IRNDPTWQGP ILAPGLINRS TEITGPPLRN MLINALNAPV NTYMTDFEDS ASPTWNNMVY GQVNLYDAIR NQIDFDTPRK SYKLNGNVAN LPTIIVRPRG WHMVEKHLYV DDEPISASIF DFGLYFYHNA KELIKLGKGP YFYLPKMEHH LEAKLWNDVF CVAQDYIGIP RGTIRATVLI ETLPAAFQME EIIYQLRQHS SGLNCGRWDY IFSTIKRLRN DPNHILPNRN QVTMTSPFMD AYVKRLINTC HRRGVHAMGG MAAQIPIKDD PAANEKAMTK VRNDKIRELT NGHDGSWVAH PALAPICNEV FINMGTPNQI YFIPENVVTA ANLLETKIPN GEITTEGIVQ NLDIGLQYME AWLRGSGCVP INNLMEDAAT AEVSRCQLYQ WVKHGVTLKD TGEKVTPELT EKILKEQVER LSKASPLGDK NKFALAAKYF LPEIRGEKFS EFLTTLLYDE IVSTKATPTD LSKL // ID MASZ_YEAST STANDARD; PRT; 554 AA. AC P21826; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Malate synthase 2, glyoxysomal (EC 4.1.3.2). GN MSL2 OR DAL7 OR YIR031C. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=RH218; RX MEDLINE=90014776; PubMed=2552287; RA Yoo H.S., Cooper T.G.; RT "The DAL7 promoter consists of multiple elements that cooperatively RT mediate regulation of the gene's expression."; RL Mol. Cell. Biol. 9:3231-3243(1989). RN [2] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=93215849; PubMed=8462696; RA Fernandez E., Fernandez M., Rodicio R.; RT "Two structural genes are encoding malate synthase isoenzymes in RT Saccharomyces cerevisiae."; RL FEBS Lett. 320:271-275(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA Barrell B.G., Badcock K., Bankier A.T., Bowman S., Brown D., RA Churcher C.M., Connor R., Copsey T., Dear S., Devlin K., Fraser A., RA Gentles S., Hamlyn N., Horsnell T.S., Hunt S., Jagels K., Jones M., RA Louis E., Lye G., Moule S., Moule T., Odell C., Pearson D., RA Rajandream M.A., Riles L., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS ISOZYME IS INVOLVED IN THE DEGRADATION OF ALLANTOIN CC (PURINE CATABOLISM). CC -!- CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O + CC GLYOXYLATE. CC -!- PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE CC TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS). CC -!- SUBUNIT: HOMOTRIMER. CC -!- SUBCELLULAR LOCATION: GLYOXYSOMAL. CC -!- INDUCTION: BY ALLOPHANATE OR OXALURATE. CC -!- SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28124; AAA50351.1; -. DR EMBL; Z38061; CAA86191.1; -. DR PIR; A32823; A32823. DR PIR; S32413; S32413. DR SGD; S0001470; DAL7. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Glyoxylate bypass; Tricarboxylic acid cycle; Lyase; Glyoxysome; KW Multigene family; Purine metabolism. FT SITE 552 554 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 115 115 D -> A (IN REF. 3). FT CONFLICT 166 166 G -> D (IN REF. 3). FT CONFLICT 302 302 N -> P (IN REF. 3). SQ SEQUENCE 554 AA; 62797 MW; E9221758A0FE67A0 CRC64; MVKISLDNTA LYADIDTTPQ FEPSKTTVAD ILTKDALEFI VLLHRTFNST RKQLLANRSN LQSKLDSGEY RFDFLPETEQ IRNDPTWQGA IPAPGLINRS SEITGPPLRN MLVNDLNAEV TTYMTDFEDS SSPTWENMIY GQVNLYDAIR NQIDFKTPRK EYRLKGDISR LPTLIVRPRG WHMVEKHLYI DDEPISASIF DFGLYFYHNA KELVKIGKGP YFYLPKMEHH MEVKLWNDIF CVAQDFIGMP RGTIRATVLI ETLPAAFQME EIIYQIREHS SGLNCGRWDY IFSTIKKLRN LNEHVLPNRD LVTMTSPFMD AYVKRLINTC HRRGVHAMGG MAAQIPIKDD PKANEAAMNK VRNDKIREMK NGHDGSWVAH PALAPICNEV FSNMGTANQI YFVPDVHVTS SDLLNTKIQD AQVTTEGIRV NLDIGLQYME AWLRGSGCVP INHLMEDAAT AEVSRCQLYQ WVKHGVVLSD TGDKVTPELT AKILNEETAK LASASPLGEK NKFALAAKYF LPEVTGKIFS DFLTTLLYDE IIKPSAKPVD LSKL // ID G3PG_LEIME STANDARD; PRT; 360 AA. AC Q27890; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase, glycosomal (EC 1.2.1.12) DE (GAPDH). GN GAPG. OS Leishmania mexicana. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania. OX NCBI_TaxID=5665; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SSP. MEXICANA; RX MEDLINE=93063042; PubMed=1435864; RA Hannaert V., Blaauw M., Kohl L., Allert S., Opperdoes F.R., RA Michels P.A.M.; RT "Molecular analysis of the cytosolic and glycosomal glyceraldehyde-3- RT phosphate dehydrogenase in Leishmania mexicana."; RL Mol. Biochem. Parasitol. 55:115-126(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=96072735; PubMed=7578111; RA Kim H., Feil I.K., Verlinde C.L.M.J., Petra P.H., Hol W.G.J.; RT "Crystal structure of glycosomal glyceraldehyde-3-phosphate RT dehydrogenase from Leishmania mexicana: implications for structure- RT based drug design and a new position for the inorganic phosphate RT binding site."; RL Biochemistry 34:14975-14986(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=98239713; PubMed=9571030; RA Kim H., Hol W.G.J.; RT "Crystal structure of Leishmania mexicana glycosomal glyceraldehyde-3- RT phosphate dehydrogenase in a new crystal form confirms the putative RT physiological active site structure."; RL J. Mol. Biol. 278:5-11(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS). RX MEDLINE=99218270; PubMed=10200252; RA Aronov A.M., Suresh S., Buckner F.S., van Voorhis W.C., Verlinde C.L., RA Opperdoes F.R., Hol W.G.J., Gelb M.H.; RT "Structure-based design of submicromolar, biologically active RT inhibitors of trypanosomatid glyceraldehyde-3-phosphate RT dehydrogenase."; RL Proc. Natl. Acad. Sci. U.S.A. 96:4273-4278(1999). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: GLYCOSOMAL. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65226; CAA46334.1; -. DR EMBL; X65226; CAA46333.1; -. DR PDB; 1GYP; 07-DEC-95. DR PDB; 1GYQ; 16-MAR-99. DR PDB; 1A7K; 17-JUN-98. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Glycosome; 3D-structure. FT INIT_MET 0 0 FT BINDING 166 166 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 194 194 ACTIVATES THIOL GROUP DURING CATALYSIS. FT SITE 358 360 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 360 AA; 38901 MW; A60FF1FD4E9513BE CRC64; APIKVGINGF GRIGRMVFQA ICDQGLIGTE IDVVAVVDMS TNAEYFAYQM KHDTVHGRPK YTVEAVKSSP SVETADVLVV NGHRIKCVKA QRNPADLPWG KLGVDYVIES TGLFTDKLKA EGHIKGGAKK VVISAPASGG AKTIVMGVNQ HEYSPASHHV VSNASCTTNC LAPIVHVLTK ENFGIETGLM TTIHSYTATQ KTVDGVSLKD WRGGRAAAVN IIPSTTGAAK AVGMVIPSTK GKLTGMSFRV PTPDVSVVDL TFRATRDTSI QEIDKAIKKA AQTYMKGILG FTDEELVSAD FINDNRSSVY DSKATLQNNL PGEKRFFKVV SWYDNEWAYS HRVVDLVRYM AAKDAASSKM // ID G3PG_TRYBB STANDARD; PRT; 358 AA. AC P22512; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase, glycosomal (EC 1.2.1.12) DE (GAPDH). OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE OF 1-52. RC STRAIN=427; RX MEDLINE=86247562; PubMed=3013612; RA Michels P.A.M., Poliszczak A., Osinga K.A., Misset O., RA van Beeuman J., Wiegenga R.K., Borst P., Opperdoes F.R.; RT "Two tandemly linked identical genes code for the glycosomal RT glyceraldehyde-phosphate dehydrogenase in Trypanosoma brucei."; RL EMBO J. 5:1049-1056(1986). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS). RX MEDLINE=93211960; PubMed=8460146; RA Vellieux F.M., Hajdu J., Verlinde C.L., Groendijk H., Read R.J., RA Greenhough T.J., Campbell J.W., Kalk K.H., Littlechild J.A., RA Watson H.C.; RT "Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase RT from Trypanosoma brucei determined from Laue data."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2355-2359(1993). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: GLYCOSOMAL. CC -!- MISCELLANEOUS: THERE ARE TWO IDENTICAL GENES THAT CODES FOR CC GLYCOSOMAL GAPDH. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59955; CAA42576.1; -. DR EMBL; X59955; CAA42577.1; -. DR EMBL; M26816; AAA30198.1; -. DR PIR; S18806; DEUT1B. DR PIR; S18807; S18807. DR PDB; 1GGA; 31-JAN-94. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glycolysis; Oxidoreductase; NAD; Glycosome; Multigene family; KW 3D-structure. FT INIT_MET 0 0 FT BINDING 165 165 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 193 193 ACTIVATES THIOL GROUP DURING CATALYSIS. FT SITE 356 358 MICROBODY TARGETING SIGNAL (POTENTIAL). FT STRAND 2 7 FT TURN 11 11 FT HELIX 12 22 FT TURN 23 24 FT STRAND 26 26 FT TURN 27 29 FT STRAND 30 37 FT HELIX 42 50 FT STRAND 51 52 FT TURN 53 55 FT STRAND 56 57 FT STRAND 62 65 FT TURN 69 70 FT STRAND 76 79 FT TURN 80 81 FT STRAND 82 88 FT HELIX 93 95 FT HELIX 98 101 FT TURN 102 102 FT STRAND 105 108 FT STRAND 115 115 FT HELIX 116 124 FT TURN 125 126 FT STRAND 129 132 FT STRAND 137 137 FT STRAND 141 142 FT TURN 145 150 FT TURN 154 156 FT STRAND 159 161 FT HELIX 165 179 FT TURN 180 181 FT STRAND 186 194 FT TURN 197 198 FT HELIX 210 213 FT HELIX 216 218 FT STRAND 221 224 FT HELIX 227 234 FT HELIX 236 238 FT TURN 239 240 FT STRAND 242 249 FT STRAND 255 262 FT HELIX 269 281 FT TURN 282 287 FT STRAND 288 291 FT HELIX 297 300 FT TURN 301 302 FT STRAND 307 310 FT HELIX 311 316 FT TURN 317 317 FT TURN 320 321 FT STRAND 325 332 FT TURN 334 335 FT HELIX 336 352 FT TURN 353 354 SQ SEQUENCE 358 AA; 38906 MW; 4C5100D3DA76C8D9 CRC64; TIKVGINGFG RIGRMVFQAL CDDGLLGNEI DVVAVVDMNT DARYFAYQMK YDSVHGKFKH SVSTTKSKPS VAKDDTLVVN GHRILCVKAQ RNPADLPWGK LGVEYVIEST GLFTVKSAAE GHLRGGARKV VISAPASGGA KTFVMGVNHN NYNPREQHVV SNASCTTNCL APLVHVLVKE GFGISTGLMT TVHSYTATQK TVDGVSVKDW RGGRAAALNI IPSTTGAAKA VGMVIPSTQG KLTGMAFRVP TADVSVVDLT FIATRDTSIK EIDAALKRAS KTYMKNILGY TDEELVSADF ISDSRSSIYD SKATLQNNLP NERRFFKIVS WYDNEWGYSH RVVDLVRHMA ARDRAAKL // ID G3PG_TRYCR STANDARD; PRT; 359 AA. AC P22513; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase, glycosomal (EC 1.2.1.12) DE (GAPDH). OS Trypanosoma cruzi. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5693; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=X10/6; RX MEDLINE=90360985; PubMed=2167831; RA Kendall G., Wilderspin A.F., Ashall F., Miles M.A., Kelly J.M.; RT "Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate RT dehydrogenase does not conform to the 'hotspot' topogenic signal RT model."; RL EMBO J. 9:2751-2758(1990). CC -!- CATALYTIC ACTIVITY: D-GLYCERALDEHYDE 3-PHOSPHATE + ORTHOPHOSPHATE CC + NAD(+) = 1,3-DIPHOSPHATEGLYCERATE + NADH. CC -!- PATHWAY: FIRST STEP IN THE SECOND PHASE OF GLYCOLYSIS. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- SUBCELLULAR LOCATION: GLYCOSOMAL. CC -!- MISCELLANEOUS: THERE ARE TWO IDENTICAL GENES THAT CODES FOR CC GLYCOSOMAL GAPDH. CC -!- SIMILARITY: BELONGS TO THE GLYCERALDEHYDE 3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52898; CAA37080.1; -. DR EMBL; X52898; CAA37079.1; -. DR PIR; S12565; DEUT1C. DR PIR; S16508; S16508. DR HSSP; P22512; 1GGA. DR InterPro; IPR000173; GAP_DH. DR Pfam; PF00044; gpdh; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR PROSITE; PS00071; GAPDH; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Glycolysis; Oxidoreductase; NAD; Glycosome; Multigene family. FT BINDING 166 166 GLYCERALDEHYDE 3-PHOSPHATE. FT ACT_SITE 194 194 ACTIVATES THIOL GROUP DURING CATALYSIS. FT SITE 357 359 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 359 AA; 39060 MW; 741ED29A4426453B CRC64; MPIKVGINGF GRIGRMVFQA LCEDGLLGTE IDVVAVVDMN TDAEYFAYQM RYDTVHGKFK YEVTTTKSSP SVAKDDTLVV NGHRILCVKA QRNPADLPWG KLGVEYVIES TGLFTAKAAA EGHLRGGARK VVISAPASGG AKTLVMGVNH HEYNPSEHHV VSNASCTTNC LAPIVHVLVK EGFGVQTGLM TTIHSYTATQ KTVDGVSVKD WRGGRAAAVN IIPSTTGAAK AVGMVIPSTQ GKLTGMSFRV PTPDVSVVDL TFTAARDTSI QEIDAALKRA SKTYMKGILG YTDEELVSAD FINDNRSSIY DSKATLQNNL PKERRFFKIV SWYDNEWGYS HRVVDLVRHM ASKDRSARL // ID G6PI_TRYBB STANDARD; PRT; 607 AA. AC P13377; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-DEC-1992 (Rel. 24, Last annotation update) DE Glucose-6-phosphate isomerase, glycosomal (GPI) (EC 5.3.1.9) DE (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI). GN PGI. OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=427; RX MEDLINE=90005496; PubMed=2792108; RA Marchand M., Kooystra U., Wierenga R.K., Lambeir A.M., van Beeumen J., RA Opperdoes F.R., Michels P.A.M.; RT "Glucosephosphate isomerase from Trypanosoma brucei. Cloning and RT characterization of the gene and analysis of the enzyme."; RL Eur. J. Biochem. 184:455-464(1989). CC -!- CATALYTIC ACTIVITY: GLUCOSE 6-PHOSPHATE = FRUCTOSE 6-PHOSPHATE. CC -!- PATHWAY: INVOLVED IN GLYCOLYSIS AND IN GLUCONEOGENESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: GLYCOSOMAL. CC -!- SIMILARITY: BELONGS TO THE GPI FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15540; CAA33547.1; -. DR PIR; S06113; NUUTB. DR InterPro; IPR001672; G6P_Isomerase. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Gluconeogenesis; Glycolysis; Isomerase; Glycosome. FT SITE 605 607 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 607 AA; 67518 MW; AB237B7261CF2B74 CRC64; MSSYLDDLRI DLAASPASGG SASIAVGSFN IPYEVTRRLK GVGADADTTL TSCASWTQLQ KLYEQYGDEP IKKHFEADSE RGQRYSVKVS LGSKDENFLF LDYSKSHIND EIKCALLRLA EERGIRQFVQ SVFRGERVNT TENRPVLHIA LRNRSNRPIY VDGKDVMPAV NKVLDQMRSF SEKVRTGEWK GHTGKAIRHV VNIGIGGSDL GPVMATEALK PFSQRDLSLH FVSNVDGTHI AEVLKSIDIE ATLFIVASKT FTTQETITNA LSARRALLDY LRSRGIDEKG SVAKHFVALS TNNQKVKEFG IDEENMFQFW DWVGGRYSMW SAIGLPIMIS IGYENFVELL TGAHVIDEHF ANAPPEQNVP LLLALVGVWY INFFGAVTHA ILPYDQYLWR LPAYLQQLDM ESNGKYVTRS GKTVSTLTGP IIFGEAGTNG QHAFYQLIHQ GTNLIPCDFI GAIQSQNKIG DHHKIFMSNF FAQTEALMIG KSPSEVRREL EAAGERSAEK INALLPHKTF IGGRPSNTLL IKSLTPRALG AIIAMYEHKV LVQGAIWGID SYDQWGVELG KVLAKSILPQ LRPGMRVNNH DSSTNGLINM FNELSHL // ID GPDA_TRYBB STANDARD; PRT; 354 AA. AC P90593; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal (EC 1.1.1.8). GN GPD. OS Trypanosoma brucei brucei. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=427; RX MEDLINE=97077437; PubMed=8920004; RA Kohl L., Drmota T., Thi C.D., Callens M., van Beeumen J., RA Opperdoes F.R., Michels P.A.M.; RT "Cloning and characterization of the NAD-linked glycerol-3-phosphate RT dehydrogenases of Trypanosoma brucei brucei and Leishmania mexicana RT mexicana and expression of the trypanosome enzyme in Escherichia RT coli."; RL Mol. Biochem. Parasitol. 76:159-173(1996). CC -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(P)(+) = CC GLYCERONE PHOSPHATE + NAD(P)H. CC -!- SUBCELLULAR LOCATION: GLYCOSOMAL. CC -!- SIMILARITY: BELONGS TO THE NAD-DEPENDENT GLYCEROL-3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X89738; CAA61890.1; -. DR InterPro; IPR001652; NAD_Gly3P_dh. DR Pfam; PF01210; NAD_Gly3P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR ProDom; PD001649; NAD_Gly3P_dh; 1. DR PROSITE; PS00957; NAD_G3PDH; FALSE_NEG. KW Oxidoreductase; NAD; Glycosome. FT SITE 352 354 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 354 AA; 37783 MW; 12CE19AEDA9E4EC9 CRC64; MVSGVTYLKR GAVFGSGAFG TALACVLAKK CESVSVWHMN ANEARVVNQK HENVYFLPGA PLPANLTFTA DAEECAKGAE IVLFVIPTQF LRGFLQKNSH ILRNHVVSRN VPVVMCSKGI ERSSLLFPAQ ILEEFLPNYP IGVIAGPSFA IEVAKGMLTN VCTAAADINM ARKIQRIMTT SDGSFRCWAT TDVIGCEIAS AMKNVLAIAS GALKGLGTEN NARAALISRG LLEIRDLTLA LGGTGEAVFG LPGLGDLLLT CSSELSRNFT VGMKLGQGIS LEEIKRTSKA VAEGVATAEP LERLAKKHNA DLPICHEVYN VLYANGCAKR SFKKLNSCKL ADEGLPALPR TSKM // ID GPDA_TRYBR STANDARD; PRT; 354 AA. AC Q26756; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Glycerol-3-phosphate dehydrogenase [NAD+], glycosomal (EC 1.1.1.8). GN GPD. OS Trypanosoma brucei rhodesiense. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=31286; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=VITAT 1.1; RX MEDLINE=97077436; PubMed=8920003; RA Stebeck C.E., Frevert U., Mommsen T.P., Vassella E., Roditi I., RA Pearson T.W.; RT "Molecular characterization of glycosomal NAD(+)-dependent glycerol 3- RT phosphate dehydrogenase from Trypanosoma brucei rhodesiense."; RL Mol. Biochem. Parasitol. 76:145-158(1996). CC -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(P)(+) = CC GLYCERONE PHOSPHATE + NAD(P)H. CC -!- SUBCELLULAR LOCATION: GLYCOSOMAL. CC -!- SIMILARITY: BELONGS TO THE NAD-DEPENDENT GLYCEROL-3-PHOSPHATE CC DEHYDROGENASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X91142; CAA62581.1; -. DR InterPro; IPR001652; NAD_Gly3P_dh. DR Pfam; PF01210; NAD_Gly3P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR ProDom; PD001649; NAD_Gly3P_dh; 1. DR PROSITE; PS00957; NAD_G3PDH; FALSE_NEG. KW Oxidoreductase; NAD; Glycosome. FT SITE 352 354 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 354 AA; 37834 MW; 0CE049C5E8F83C00 CRC64; MVSGVTYLKR GAVFGSGAFG TALACVLAKK CESVSVWHMN ANEARVVNQK HENVYFLPGA PLPANLTFTA DAEECAKGAE IVLFVIPTQF LRGFLQKNSH ILRNHVVSRN VPVVMCSKGI ERSSLLFPAQ ILEEFLPNYP IGVIAGPSFA IEVAKGMLTN VCTAAADIDM ARKIQRIMTT SDGSFRCWAT TDVIGCEIAS AMKNVLAIAS GALKGLGTEN NARAALISRG LLEIRDLTLA LGGTGEAVFG LPGLGDLLLT CSSELSRNFT VGMKLGKGIS LEEIKRTSKA VAEGVATAEP LERLAKKHNV HLPICHEVYN VLYANGCAKR SFKKLNSCKL ADEGLPALPR TSKM // ID NLTP_CHICK STANDARD; PRT; 547 AA. AC Q07598; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Nonspecific lipid-transfer protein precursor (NSL-TP) (Sterol carrier DE protein 2) (SCP-2) (Sterol carrier protein X) (SCP-X) (SCPX) DE (Fragment). GN SCP2. OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WHITE LEGHORN; TISSUE=Liver; RX MEDLINE=93312016; PubMed=8323294; RA Pfeifer S.M., Sakuragi N., Ryan A., Johnson A.L., Deeley R.G., RA Billheimer J.T., Baker M.E., Strauss J.F. III; RT "Chicken sterol carrier protein 2/sterol carrier protein x: cDNA RT cloning reveals evolutionary conservation of structure and regulated RT expression."; RL Arch. Biochem. Biophys. 304:287-293(1993). CC -!- FUNCTION: MEDIATES IN VITRO THE TRANSFER OF ALL COMMON CC PHOSPHOLIPIDS, CHOLESTEROL AND GANGLIOSIDES BETWEEN MEMBRANES. MAY CC PLAY A ROLE IN REGULATING STEROIDOGENESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC IN THE LIVER AND ALSO ASSOCIATED CC WITH MITOCHONDRIA ESPECIALLY IN STEROIDOGENIC TISSUES. SCP-X CC RESIDES IN THE PEROXISOME. CC -!- ALTERNATIVE PRODUCTS: DIFFERENTIAL INITIATION OF SCP2 GENE CC TRANSCRIPT LEADS TO THE EXPRESSION OF PRE-SCP-2 AND SCP-X FROM A CC SINGLE GENE. CC -!- TISSUE SPECIFICITY: EXPRESSED AT HIGH LEVELS IN THE LIVER, CC INTESTINE AND OVARIAN GRANULOSA CELLS. CC -!- DEVELOPMENTAL STAGE: SCP-X LEVELS REMAIN UNCHANGED DURING DAY 20 CC EMBRYO TO 4 WEEKS POSTHATCH. A 10-FOLD INCREASE IN SCP-2 LEVEL IS CC SEEN BY 1 WEEK POSTHATCH AND DECLINES SLIGHTLY BETWEEN 3 AND 4 CC WEEKS POSTHATCH. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE THIOLASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09231; AAA02488.1; -. DR InterPro; IPR003033; SCP2. DR InterPro; IPR002155; Thiolase. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF00108; thiolase; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; FALSE_NEG. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Lipid-binding; Transport; Mitochondrion; Peroxisome; Transit peptide; KW Alternative initiation. FT NON_TER 1 1 FT CHAIN <1 547 SCP-X. FT TRANSIT 408 427 MITOCHONDRION (BY SIMILARITY). FT CHAIN 428 547 NONSPECIFIC LIPID-TRANSFER PROTEIN (BY FT SIMILARITY). FT INIT_MET 408 408 FOR NSL-TP. FT ACT_SITE 97 97 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 494 494 ESSENTIAL FOR TRANSPORT OF LIPIDS (BY FT SIMILARITY). FT SITE 545 547 MICROBODY TARGETING SIGNAL (POTENTIAL). SQ SEQUENCE 547 AA; 58691 MW; CAFCDDE4A1C1B3B8 CRC64; ARVCEERGGP AAIMQRRVFV VGVGMTKFAK PSENSVDYPD LAKEAGQKAL ADAGIPYSAV EQACVGYVYG DSTCGQRAIY HGLGLTGIPI INVNNNCATG STALFMSRQL VEGGLADCVL ALGFERMAKG SLASGFSDRT NPMDKHLEIM INKYGLASAP ITPQMFANAG KEHMEKYGTN PEYFAKIAWK NHSHSTNNPY SQFQKKYTLD EVLQSRKVFD FLTVLQCCPT SNGAAAAILA SEDFVKRHKL QPQAVEILAQ VMATDYPSTF EENSCMKMVG YDMTKKAAEK CFKKAGLKPT DVDVIELHDC FSVNEFITYE ALGLCPEGKA CDLIDRGDNT YGGKWVINPS GGLISKGHPL GATGLAQSAE LCWQLRGLAG RREVGGARRA LQHNLGLGGA VVVTLYAMGF PGAASDGGVT AVPLSAAVDG FKSHLVFKEI EKKLQEEGEQ FVKKIGGVFA FKIKDGPGGK EATWVVDVKN GKGSVAVNSD KKADCTITMA DTDLLALMTG KMNPQTAFFQ GKLKISGNMG MAMKLQNLQL QPGKAKL // ID NLTP_HUMAN STANDARD; PRT; 547 AA. AC P22307; Q16622; Q15432; Q99430; DT 01-AUG-1991 (Rel. 19, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Nonspecific lipid-transfer protein precursor (NSL-TP) (Sterol carrier DE protein 2) (SCP-2) (Sterol carrier protein X) (SCP-X) (SCPX). GN SCP2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=95213031; PubMed=7698762; RA Ohba T., Rennert H., Pfeifer S.M., He Z., Yamamoto R., Holt J.A., RA Billheimer J.T., Strauss J.F. III; RT "The structure of the human sterol carrier protein X/sterol carrier RT protein 2 gene (SCP2)."; RL Genomics 24:370-374(1994). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=92029618; PubMed=1718316; RA He Z., Yamamoto R., Furth E.E., Schantz L.J., Naylor S.L., George H., RA Billheimer J.T., Strauss J.F. III; RT "cDNAs encoding members of a family of proteins related to human RT sterol carrier protein 2 and assignment of the gene to human RT chromosome 1 p21-pter."; RL DNA Cell Biol. 10:559-569(1991). RN [3] RP SEQUENCE OF 405-547 FROM N.A. RC TISSUE=Liver; RX MEDLINE=91110550; PubMed=1703300; RA Yamamoto R., Kallen C.B., Babalola G.O., Rennert H., Billheimer J.T., RA Strauss J.F. III; RT "Cloning and expression of a cDNA encoding human sterol carrier RT protein 2."; RL Proc. Natl. Acad. Sci. U.S.A. 88:463-467(1991). RN [4] RP SEQUENCE OF 405-547 FROM N.A. RC TISSUE=Liver; RX MEDLINE=93131254; PubMed=1483685; RA Yamamoto R.; RT "Localization of human sterol carrier protein 2 gene and cDNA RT expression in COS-7 cell."; RL Hokkaido Igaku Zasshi 67:839-848(1992). RN [5] RP STRUCTURE BY NMR OF SCP2. RX MEDLINE=94063072; PubMed=8243660; RA Szyperski T., Scheek S., Johansson J., Assmann G., Seedorf U., RA Wuethrich K.; RT "NMR determination of the secondary structure and the RT three-dimensional polypeptide backbone fold of the human sterol RT carrier protein 2."; RL FEBS Lett. 335:18-26(1993). CC -!- FUNCTION: MEDIATES IN VITRO THE TRANSFER OF ALL COMMON CC PHOSPHOLIPIDS, CHOLESTEROL AND GANGLIOSIDES BETWEEN MEMBRANES. MAY CC PLAY A ROLE IN REGULATING STEROIDOGENESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC IN THE LIVER AND ALSO ASSOCIATED CC WITH MITOCHONDRIA ESPECIALLY IN STEROIDOGENIC TISSUES. SCP-X CC RESIDES IN THE PEROXISOME. CC -!- ALTERNATIVE PRODUCTS: DIFFERENTIAL INITIATION OF SCP2 GENE CC TRANSCRIPT LEADS TO THE EXPRESSION OF PRE-SCP-2 AND SCP-X FROM A CC SINGLE GENE. CC -!- TISSUE SPECIFICITY: LIVER, FIBROBLASTS, AND PLACENTA. CC -!- DISEASE: SCP2 IS PRESENT IN LOW LEVELS IN SUBJECTS WITH ZELLWEGER CC SYNDROME (CEREBRO-HEPATIC-RENAL SYNDROME), WHOSE CELLS ARE CC DEFICIENT IN PEROXISOMES AND WHO HAVE AN ASSOCIATED IMPAIRMENT IN CC PLASMALOGEN AND BILE ACID SYNTHESIS AND CATABOLISM OF PHYTANIC CC ACID AND VERY-LONG-CHAIN FATTY ACIDS. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE THIOLASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11313; AAB41286.1; -. DR EMBL; U11297; AAB41286.1; JOINED. DR EMBL; U11299; AAB41286.1; JOINED. DR EMBL; U11300; AAB41286.1; JOINED. DR EMBL; U11301; AAB41286.1; JOINED. DR EMBL; U11302; AAB41286.1; JOINED. DR EMBL; U11303; AAB41286.1; JOINED. DR EMBL; U11304; AAB41286.1; JOINED. DR EMBL; U11305; AAB41286.1; JOINED. DR EMBL; U11306; AAB41286.1; JOINED. DR EMBL; U11307; AAB41286.1; JOINED. DR EMBL; U11308; AAB41286.1; JOINED. DR EMBL; U11309; AAB41286.1; JOINED. DR EMBL; U11310; AAB41286.1; JOINED. DR EMBL; U11311; AAB41286.1; JOINED. DR EMBL; U11312; AAB41286.1; JOINED. DR EMBL; M75883; AAA03557.1; -. DR EMBL; M75884; AAA03558.1; ALT_INIT. DR EMBL; M55421; AAA03559.1; ALT_SEQ. DR EMBL; S52450; AAB24921.1; -. DR PIR; A39010; A39010. DR HSSP; P27796; 1PXT. DR MIM; 184755; -. DR InterPro; IPR003033; SCP2. DR InterPro; IPR002155; Thiolase. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF00108; thiolase; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; FALSE_NEG. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Lipid-binding; Transport; Mitochondrion; Peroxisome; Transit peptide; KW Alternative initiation. FT CHAIN 1 547 SCP-X. FT TRANSIT 405 424 MITOCHONDRION (BY SIMILARITY). FT CHAIN 425 547 NONSPECIFIC LIPID-TRANSFER PROTEIN. FT INIT_MET 405 405 FOR NSL-TP. FT ACT_SITE 94 94 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 494 494 ESSENTIAL FOR TRANSPORT OF LIPIDS. FT SITE 545 547 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 10 10 T -> A (IN REF. 1). FT CONFLICT 393 393 G -> D (IN REF. 1). FT CONFLICT 472 472 A -> D (IN REF. 3 AND 4). FT CONFLICT 482 482 K -> Q (IN REF. 3 AND 4). FT CONFLICT 501 501 D -> A (IN REF. 3 AND 4). FT CONFLICT 522 522 K -> P (IN REF. 3 AND 4). SQ SEQUENCE 547 AA; 58993 MW; 29F7551465C7143A CRC64; MSSSPWEPAT LRRVFVVGVG MTKFVKPGAE NSRDYPDLAE EAGKKALADA QIPYSAVDQA CVGYVFGDST CGQRAIYHSL GMTGIPIINV NNNCATGSTA LFMARQLIQG GVAECVLALG FEKMSKGSLG IKFSDRTIPT DKHVDLLINK YGLSAHPVAP QMFGYAGKEH MEKYGTKIEH FAKIGWKNHK HSVNNPYSQF QDEYSLDEVM ASKEVFDFLT ILQCCPTSDG AAAAILASEA FVQKYGLQSK AVEILAQEMM TDLPSSFEEK SIIKMVGFDM SKEAARKCYE KSGLTPNDID VIELHDCFST NELLTYEALG LCPEGQGATL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGIGGAVVV TLYKMGFPEA ASSFRTHQIE AVPTSSASDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA DSDFLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL QPGNAKL // ID NLTP_MOUSE STANDARD; PRT; 547 AA. AC P32020; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Nonspecific lipid-transfer protein precursor (NSL-TP) (Sterol carrier DE protein 2) (SCP-2) (Sterol carrier protein X) (SCP-X) (SCPX). GN SCP2 OR SCP-2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=93154580; PubMed=8428655; RA Seedorf U., Raabe M., Assmann G.; RT "Cloning, expression and sequences of mouse sterol-carrier protein-x- RT encoding cDNAs and a related pseudogene."; RL Gene 123:165-172(1993). RN [2] RP SEQUENCE OF 405-547 FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=91236770; PubMed=1709640; RA Moncecchi D.T., Pastuszyn A., Scallen T.J.; RT "cDNA sequence and bacterial expression of mouse liver sterol carrier RT protein-2."; RL J. Biol. Chem. 266:9885-9892(1991). RN [3] RP SEQUENCE OF 1-23 FROM N.A. RC STRAIN=129/SV; TISSUE=Liver; RX MEDLINE=96354847; PubMed=8751375; RA Raabe M., Seedorf U., Hameister H., Ellinghaus P., Assmann G.; RT "Structure and chromosomal assignment of the murine sterol carrier RT protein 2 gene (Scp2) and two related pseudogenes by in situ RT hybridization."; RL Cytogenet. Cell Genet. 73:279-281(1996). CC -!- FUNCTION: MEDIATES IN VITRO THE TRANSFER OF ALL COMMON CC PHOSPHOLIPIDS, CHOLESTEROL AND GANGLIOSIDES BETWEEN MEMBRANES. MAY CC PLAY A ROLE IN REGULATING STEROIDOGENESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC IN THE LIVER AND ALSO ASSOCIATED CC WITH MITOCHONDRIA ESPECIALLY IN STEROIDOGENIC TISSUES. SCP-X CC RESIDES IN THE PEROXISOME. CC -!- ALTERNATIVE PRODUCTS: DIFFERENTIAL INITIATION OF SCP2 GENE CC TRANSCRIPT LEADS TO THE EXPRESSION OF PRE-SCP-2 AND SCP-X FROM A CC SINGLE GENE. CC -!- TISSUE SPECIFICITY: PRESENT AT LOW LEVELS IN ALL TISSUES CC EXAMINED BUT EXPRESSED PREDOMINANTLY IN THE LIVER. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE THIOLASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M91458; AAA40098.1; -. DR EMBL; M62361; AAA40099.1; -. DR EMBL; X91150; CAA62592.1; -. DR PIR; A40015; A40015. DR PIR; JU0157; JU0157. DR MGD; MGI:98254; Scp2. DR InterPro; IPR003033; SCP2. DR InterPro; IPR002155; Thiolase. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF00108; thiolase; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; FALSE_NEG. DR PROSITE; PS00342; MICROBODIES_CTER; 1. KW Lipid-binding; Transport; Mitochondrion; Peroxisome; Transit peptide; KW Alternative initiation. FT CHAIN 1 547 SCP-X. FT TRANSIT 405 424 MITOCHONDRION (POTENTIAL). FT CHAIN 425 547 NONSPECIFIC LIPID-TRANSFER PROTEIN. FT INIT_MET 405 405 FOR NSL-TP. FT ACT_SITE 94 94 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 494 494 ESSENTIAL FOR TRANSPORT OF LIPIDS (BY FT SIMILARITY). FT SITE 545 547 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 478 478 V -> A (IN REF. 2). SQ SEQUENCE 547 AA; 59158 MW; BAB02F986D16B18E CRC64; MPSVALKSPR LRRVFVVGVG MTKFMKPGGE NSRDYPDMAK EAGQKALEDA QIPYSAVEQA CVGYVYGDST SGQRAIYHSL GLTGIPIINV NNNCSTGSTA LFMAHQLIQG GLANCVLALG FEKMERGSIG TKFSDRTTPT DKHIEVLIDK YGLSAHPITP QMFGYAGKEH MEKYGTKVEH FAKIGWKNHK HSVNNTYSQF QDEYSLEEVM KSKPVFDFLT ILQCCPTSDG ACAAILSSEE FVQQYGLQSK AVEIVAQEMM TDLPSTFEEK SIIKVVGYDM SKEAARRCYE KSGLTPNDVD VIELHDCFSV NELITYEALG LCPEGQGGTL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAVVV TLYRMGFPEA ASSFRTHQVS AAPTSSAGDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPNSD KKADCTITMA DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQNLQL QPGKAKL // ID NLTP_RAT STANDARD; PRT; 547 AA. AC P11915; Q63383; DT 01-OCT-1989 (Rel. 12, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Nonspecific lipid-transfer protein precursor (NSL-TP) (Sterol carrier DE protein 2) (SCP-2) (Sterol carrier protein X) (SCP-X) (SCPX). GN SCP2 OR SCP-2. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Liver; RX MEDLINE=91093192; PubMed=1985920; RA Seedorf U., Assmann G.; RT "Cloning, expression, and nucleotide sequence of rat liver sterol RT carrier protein 2 cDNAs."; RL J. Biol. Chem. 266:630-636(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91239563; PubMed=2034675; RA Mori T., Tsukamoto T., Mori H., Tashiro Y., Fujiki Y.; RT "Molecular cloning and deduced amino acid sequence of nonspecific RT lipid transfer protein (sterol carrier protein 2) of rat liver: a RT higher molecular mass (60 kDa) protein contains the primary sequence RT of nonspecific lipid transfer protein as its C-terminal part."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4338-4342(1991). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=92007881; PubMed=1915369; RA Ossendorp B.C., van Heusden G.P.H., de Beer A.L.J., Bos K., RA Schouten G.L., Wirtz K.W.A.; RT "Identification of the cDNA clone which encodes the 58-kDa protein RT containing the amino acid sequence of rat liver non-specific lipid- RT transfer protein (sterol-carrier protein 2). Homology with rat RT peroxisomal and mitochondrial 3-oxoacyl-CoA thiolases."; RL Eur. J. Biochem. 201:233-239(1991). RN [4] RP SEQUENCE OF 33-547 FROM N.A. RC TISSUE=Liver; RX MEDLINE=90241231; PubMed=2334427; RA Ossendorp B.C., van Heusden G.P.H., Wirtz K.W.A.; RT "The amino acid sequence of rat liver non-specific lipid transfer RT protein (sterol carrier protein 2) is present in a high molecular RT weight protein: evidence from cDNA analysis."; RL Biochem. Biophys. Res. Commun. 168:631-636(1990). RN [5] RP SEQUENCE OF 275-547 FROM N.A. RC STRAIN=CD; TISSUE=Liver; RX MEDLINE=90253610; PubMed=2340090; RA Billheimer J.T., Strehl L.L., Davis G.L., Strauss J.F. III, RA Davis L.G.; RT "Characterization of a cDNA encoding rat sterol carrier protein2."; RL DNA Cell Biol. 9:159-165(1990). RN [6] RP SEQUENCE OF 425-547. RC TISSUE=Liver; RX MEDLINE=88007528; PubMed=3115977; RA Pastuszyn A., Noland B.J., Bazan J.F., Fletterick R.J., Scallen T.J.; RT "Primary sequence and structural analysis of sterol carrier protein 2 RT from rat liver: homology with immunoglobulins."; RL J. Biol. Chem. 262:13219-13227(1987). RN [7] RP SEQUENCE OF 425-547. RC TISSUE=Liver; RX MEDLINE=88280812; PubMed=3395344; RA Morris H.R., Larsen B.S., Billheimer J.T.; RT "A mass spectrometric study of the structure of sterol carrier RT protein SCP2 from rat liver."; RL Biochem. Biophys. Res. Commun. 154:476-482(1988). CC -!- FUNCTION: MEDIATES IN VITRO THE TRANSFER OF ALL COMMON CC PHOSPHOLIPIDS, CHOLESTEROL AND GANGLIOSIDES BETWEEN MEMBRANES. MAY CC PLAY A ROLE IN REGULATING STEROIDOGENESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC IN THE LIVER AND ALSO ASSOCIATED CC WITH MITOCHONDRIA ESPECIALLY IN STEROIDOGENIC TISSUES. SCP-X CC RESIDES IN THE PEROXISOME. CC -!- ALTERNATIVE PRODUCTS: DIFFERENTIAL INITIATION OF SCP2 GENE CC TRANSCRIPT LEADS TO THE EXPRESSION OF PRE-SCP-2 AND SCP-X FROM A CC SINGLE GENE. CC -!- TISSUE SPECIFICITY: LIVER > INTESTINE > BRAIN > LUNG, COLON, CC STOMACH, SPLEEN, KIDNEY, HEART, AND OVARY. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE THIOLASE CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M62763; AAA40622.1; -. DR EMBL; M62763; AAA40623.1; ALT_INIT. DR EMBL; M57454; AAA42121.1; -. DR EMBL; M57453; AAA42122.1; -. DR EMBL; M58287; AAA41726.1; -. DR EMBL; M34728; AAA42120.1; -. DR EMBL; X60654; CAA43060.1; ALT_INIT. DR EMBL; X60654; CAA43061.1; -. DR PIR; A27661; A27661. DR PIR; A29366; A29366. DR PIR; A34584; A34584. DR PIR; A34635; A34635. DR PIR; A39054; A39054. DR InterPro; IPR003033; SCP2. DR InterPro; IPR002155; Thiolase. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF00108; thiolase; 1. DR PROSITE; PS00099; THIOLASE_3; FALSE_NEG. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00737; THIOLASE_2; 1. KW Lipid-binding; Transport; Mitochondrion; Peroxisome; Transit peptide; KW Alternative initiation. FT CHAIN 1 547 SCP-X. FT TRANSIT 405 424 MITOCHONDRION (POTENTIAL). FT CHAIN 425 547 NONSPECIFIC LIPID-TRANSFER PROTEIN. FT INIT_MET 405 405 FOR NSL-TP. FT ACT_SITE 94 94 SUBSTRATE BINDING (BY SIMILARITY). FT SITE 494 494 ESSENTIAL FOR TRANSPORT OF LIPIDS. FT SITE 545 547 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 12 12 P -> R (IN REF. 2). FT CONFLICT 50 50 R -> A (IN REF. 2). FT CONFLICT 265 265 S -> T (IN REF. 1). FT CONFLICT 427 428 AG -> SV (IN REF. 7). FT CONFLICT 436 436 I -> V (IN REF. 7). FT CONFLICT 446 446 E -> D (IN REF. 7). FT CONFLICT 450 450 E -> Q (IN REF. 7). FT CONFLICT 488 488 D -> N (IN REF. 7). FT CONFLICT 516 516 S -> T (IN REF. 7). FT CONFLICT 526 526 A -> N (IN REF. 7). FT CONFLICT 537 537 S -> N (IN REF. 7). FT CONFLICT 543 543 D -> G (IN REF. 7). SQ SEQUENCE 547 AA; 58813 MW; D0D1B435D2DC6AFB CRC64; MPSVALNSPR LPRVFVVGVG MTKFMKPGGE NSRDYPDLAK EAGQKALADR QIPYSAVEQA CVGYVYGEST CGQRAIYHSL GLTGIPIINV NNNCSTGSTA LFMAQQLVQG GLANCVLALG FEKMEKGSLG TKYSDRSNPL EKHIDVLINK YGMSACPFAP QLFGSAGKEH METYGTKVEH FAKIGWKNHK HSVNNPYSQF QDEYSLDEIM KSRPVFDFLT VLQCCPTSDG AAAAIVSSEE FVQKHGLQSK AVEIVAQEMV TDMPSTFEEK SVIKMVGYDM SKEAARKCYE KSGLGPSDVD VIELHDCFST NELLTYEALG LCPEGQGGAL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAAVV TLYRMGFPEA ASSFRTHQIS AAPTSSAGDG FKANLIFKEI EKKLEEEGEE FVKKIGGIFA FKVKDGPGGK EATWVVDVKN GKGSVLPDSD KKADCTITMA DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQSLQL QPDKAKL // ID DCMC_ANSAN STANDARD; PRT; 504 AA. AC P12617; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Malonyl-CoA decarboxylase, mitochondrial precursor (EC 4.1.1.9) (MCD). GN MLYCD. OS Anser anser anser (Western graylag goose). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Anseriformes; Anatidae; Anser. OX NCBI_TaxID=8844; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Uropygial gland; RX MEDLINE=93037497; PubMed=1416987; RA Courchesne-Smith C., Jang S.-H., Shi Q., Dewille J., Sasaki G., RA Kolattukudy P.E.; RT "Cytoplasmic accumulation of a normally mitochondrial malonyl-CoA RT decarboxylase by the use of an alternate transcription start site."; RL Arch. Biochem. Biophys. 298:576-586(1992). RN [2] RP SEQUENCE OF 74-504 FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Uropygial gland; RX MEDLINE=89123482; PubMed=2914961; RA Jang S.-H., Cheesbrough T.M., Kolattukudy P.E.; RT "Molecular cloning, nucleotide sequence, and tissue distribution of RT malonyl-CoA decarboxylase."; RL J. Biol. Chem. 264:3500-3505(1989). CC -!- FUNCTION: CATALYZES THE CONVERSION OF MALONYL-COA TO ACETYL-COA. CC IN THE FATTY ACID BIOSYNTHESIS MCD SELECTIVELY REMOVES MALONYL-COA CC AND THUS ASSURES THAT METHYL-MALONYL-COA IS THE ONLY CHAIN CC ELONGATING SUBSTRATE FOR FATTY ACID SYNTHASE AND THAT FATTY ACIDS CC WITH MULTIPLE METHYL SIDE CHAINS ARE PRODUCED. CC -!- CATALYTIC ACTIVITY: MALONYL-COA = ACETYL-COA + CO(2). CC -!- PATHWAY: FATTY ACID BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (IN LIVER), CYTOPLASMIC (IN CC UROPYGIAL GLAND) AND PEROXISOMAL. CC -!- ALTERNATIVE PRODUCTS: A SINGLE NUCLEAR GENE PRODUCES BOTH FORMS CC BY USE OF ALTERNATIVE INITIATION CODONS IN THE SAME READING FRAME. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L21171; AAA49317.1; ALT_SEQ. DR PIR; A33313; A33313. KW Lyase; Decarboxylase; Fatty acid biosynthesis; Mitochondrion; KW Transit peptide; Alternative initiation; Peroxisome. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 504 MALONYL-COA DECARBOXYLASE, MITOCHONDRIAL. FT CHAIN 51 504 MALONYL-COA DECARBOXYLASE, FT CYTOPLASMIC/PEROXISOMAL. FT INIT_MET 51 51 FOR CYTOPLASMIC/PEROXISOMAL ISOFORM. FT SITE 502 504 MICROBODY TARGETING SIGNAL (POTENTIAL). FT CONFLICT 124 136 MISSING (IN REF. 2). FT CONFLICT 140 140 V -> L (IN REF. 2). SQ SEQUENCE 504 AA; 56689 MW; 683991C1F9773DF4 CRC64; MRGLRRGLSR LGPRLGPWAV PRSLRRVLRA AGPWRGQSSA GSVSERGGAS MEEVLSRSVP LLPPYETKEK APPPAERRSA EFVRYYRGLE AGSRRAELLG CLARDFGADH GRVAEFSAKV LQAREQEREQ GALLQAEDRV RYYLTPRYRA LFQHLGRLEG GLRFLVELRG DLVEGLAAKA VDGPHVKEMS GVLKNMLSEW FSTGFLNLER VTWQSPCEVL QKISDSEAVH PVRNWVDLKR RVGPYRRCYF FSHCAIPGEP LIILHVALTS DISSSIQSIV KDVESLETED AEKITTAIFY SISLAQQGLQ GVELGNHLIK RVVKELQKDL PQIEAFSSLS PIPGFTKWLV GLLSSQTKEL GRNELFTESE RQEISEITED STTETLKKLL TNSEWVKSEK LVKALHSPLM RLCAWYLYGE KHRGYALNPV ANFHLQNGAE LWRINWMGDT SPRGIAASCG MMVNYRYFLE DTASNSAAYL GTKHIKASEQ VLSFVSQFQQ NSKL // ID SPYA_CALJA STANDARD; PRT; 414 AA. AC P31029; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine--pyruvate aminotransferase, mitochondrial precursor DE (EC 2.6.1.51) (SPT) (Alanine--glyoxylate aminotransferase) DE (EC 2.6.1.44) (AGT). GN AGXT OR AGT1. OS Callithrix jacchus (Common marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Platyrrhini; Callitrichidae; OC Callithrix. OX NCBI_TaxID=9483; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92339467; PubMed=1339350; RA Purdue P.E., Lumb M.J., Danpure C.J.; RT "Molecular evolution of alanine/glyoxylate aminotransferase 1 RT intracellular targeting. Analysis of the marmoset and rabbit genes."; RL Eur. J. Biochem. 207:757-766(1992). CC -!- FUNCTION: DUAL METABOLIC ROLES OF GLUCONEOGENESIS (IN THE CC MITOCHONDRIA) AND GLYOXYLATE DETOXIFICATION (IN THE PEROXISOMES). CC -!- CATALYTIC ACTIVITY: L-SERINE + PYRUVATE = 3-HYDROXYPYRUVATE + CC L-ALANINE. CC -!- CATALYTIC ACTIVITY: L-ALANINE + GLYOXYLATE = PYRUVATE + GLYCINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX AND PEROXISOMAL. CC -!- SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84414; AAA35397.1; -. DR PIR; S24154; S24154. DR InterPro; IPR000192; Aminotransf_class_V. DR Pfam; PF00266; aminotran_5; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Peroxisome; KW Mitochondrion; Transit peptide; Alternative initiation. FT TRANSIT 1 23 MITOCHONDRION. FT CHAIN 24 414 SERINE--PYRUVATE AMINOTRANSFERASE, FT MITOCHONDRIAL ISOFORM. FT CHAIN 23 414 SERINE--PYRUVATE AMINOTRANSFERASE, FT PEROXISOMAL ISOFORM. FT INIT_MET 23 23 FOR PEROXISOMAL ISOFORM. FT BINDING 231 231 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 414 AA; 45054 MW; 604866DA42EEDDE1 CRC64; MFQALAKASA ALGPRAAGWV RTMASHQLLV APPKALLKPL SIPTRLLLGP GPSNLPPRTM AAGGLQMLGH MHKETYQIMD EIKEGIQYVF QTRNPLTLVI SGSGHCALEA ALINVLEPGD SFLVGVNGIW GQRAADIGER LGARVHPMTK DPGGHYTLQE VEEGLAQHKP VLLFLTHGES SSGVLQPLDG FGELCHRYKC LLLVDSVASL GGAPLYMDQQ GIDILYSGSQ KVLNAPPGTS LLSFSDTAKN KIYSRKTKPS SFYLDVKYLA NLWGCDGQPR MYHHTTPVVS LYSLREGLAL LSEQGLENSW RKHREAAAYL HGRLQALGLR LFVKDPALRL PTVTTVAVPT GYDWRDIVSY LIERFGIEIT GGLGPSTGKV LRIGLMGCNA TRENVDLVTE ALREALQHCP KKKL // ID SPYA_HUMAN STANDARD; PRT; 392 AA. AC P21549; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Serine--pyruvate aminotransferase (EC 2.6.1.51) (SPT) (Alanine-- DE glyoxylate aminotransferase) (EC 2.6.1.44) (AGT). GN AGXT OR AGT1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RX MEDLINE=91071216; PubMed=2253628; RA Nishiyama K., Berstein G., Oda T., Ichiyama A.; RT "Cloning and nucleotide sequence of cDNA encoding human liver serine- RT pyruvate aminotransferase."; RL Eur. J. Biochem. 194:9-18(1990). RN [2] RP SEQUENCE FROM N.A., AND VARIANTS LEU-11; MET-340 AND PH1 ARG-170. RX MEDLINE=91115929; PubMed=1703535; RA Purdue P.E., Takada Y., Danpure C.J.; RT "Identification of mutations associated with peroxisome-to- RT mitochondrion mistargeting of alanine/glyoxylate aminotransferase in RT primary hyperoxaluria type 1."; RL J. Cell Biol. 111:2341-2351(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90303236; PubMed=2363689; RA Takada Y., Kaneko N., Esumi H., Purdue P.E., Danpure C.J.; RT "Human peroxisomal L-alanine: glyoxylate aminotransferase. RT Evolutionary loss of a mitochondrial targeting signal by point RT mutation of the initiation codon."; RL Biochem. J. 268:517-520(1990). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=91257848; PubMed=2045108; RA Purdue P.E., Lumb M.J., Fox M., Griffo G., Hamon-Benais C., RA Povey S., Danpure C.J.; RT "Characterization and chromosomal mapping of a genomic clone encoding RT human alanine:glyoxylate aminotransferase."; RL Genomics 10:34-42(1991). RN [5] RP VARIANT PH1 PRO-205. RX MEDLINE=91248187; PubMed=2039493; RA Nishiyama K., Funai T., Katafuchi R., Hattori F., Onoyama K., RA Ichiyama A.; RT "Primary hyperoxaluria type I due to a point mutation of T to C in RT the coding region of the serine:pyruvate aminotransferase gene."; RL Biochem. Biophys. Res. Commun. 176:1093-1099(1991). RN [6] RP VARIANT PH1 GLU-82. RX MEDLINE=92250048; PubMed=1349575; RA Purdue P.E., Lumb M.J., Allsop J., Minatogawa Y., Danpure C.J.; RT "A glycine-to-glutamate substitution abolishes alanine:glyoxylate RT aminotransferase catalytic activity in a subset of patients with RT primary hyperoxaluria type 1."; RL Genomics 13:215-218(1992). RN [7] RP VARIANT PH1 PHE-187. RX MEDLINE=93244806; PubMed=1301173; RA Minatogawa Y., Tone S., Allsop J., Purdue P.E., Takada Y., RA Danpure C.J., Kido R.; RT "A serine-to-phenylalanine substitution leads to loss of RT alanine:glyoxylate aminotransferase catalytic activity and RT immunoreactivity in a patient with primary hyperoxaluria type 1."; RL Hum. Mol. Genet. 1:643-644(1992). RN [8] RP VARIANTS PH1 ARG-41 AND ILE-152. RX MEDLINE=93318842; PubMed=8101040; RA Danpure C.J., Purdue P.E., Fryer P., Griffiths S., Allsop J., RA Lumb M.J., Guttridge K.M., Jennings P.R., Scheinman J.I., Mauer S.M., RA Davidson N.O.; RT "Enzymological and mutational analysis of a complex primary RT hyperoxaluria type 1 phenotype involving alanine:glyoxylate RT aminotransferase peroxisome-to-mitochondrion mistargeting and RT intraperoxisomal aggregation."; RL Am. J. Hum. Genet. 53:417-432(1993). RN [9] RP REVIEW ON PH1. RX MEDLINE=93283455; PubMed=8507692; RA Danpure C.J.; RT "Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion RT mistargeting of alanine:glyoxylate aminotransferase."; RL Biochimie 75:309-315(1993). RN [10] RP VARIANTS PH1 CYS-233; HIS-233 AND THR-244. RX MEDLINE=97335604; PubMed=9192270; RA von Schnakenburg C., Rumsby G.; RT "Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of RT the AGXT gene."; RL J. Med. Genet. 34:489-492(1997). RN [11] RP VARIANTS PH1 VAL-41; GLU-95 INS; ARG-116 AND ARG-156. RX MEDLINE=99320862; PubMed=10394939; RA Amoroso A., Pirulli D., Puzzer D., Ferri L., Crovella S., RA Ferrettini C., Marangella M., Mazzola G., Florian F.; RT "Gene symbol: AGXT. Disease: primary hyperoxaluria type I."; RL Hum. Genet. 104:441-441(1999). RN [12] RP VARIANTS PH1 ILE-152; ARG-170; ASN-183; CYS-233 AND THR-244. RX MEDLINE=20321302; PubMed=10862087; RA Basmaison O., Rolland M.-O., Cochat P., Bozon D.; RT "Identification of 5 novel mutations in the AGXT gene."; RL Hum. Mutat. 15:577-577(2000). CC -!- CATALYTIC ACTIVITY: L-SERINE + PYRUVATE = 3-HYDROXYPYRUVATE + CC L-ALANINE. CC -!- CATALYTIC ACTIVITY: L-ALANINE + GLYOXYLATE = PYRUVATE + GLYCINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. EXCEPT IN SOME PH1 PATIENTS CC WHERE AGT IS FOUND IN THE MITOCHONDRIAL MATRIX. TO BE MISTARGETED CC AGT MUST HAVE BOTH THE LEU-11 AND ARG-170 VARIANTS. CC -!- TISSUE SPECIFICITY: LIVER. CC -!- DISEASE: DEFECTS IN AGXT ARE THE CAUSE OF PRIMARY HYPEROXALURIA CC TYPE I (PH1) (OR OXALOSIS I), AN INBORN ERROR OF GLYOXYLATE CC METABOLISM CHARACTERIZED BY INCREASED EXCRETION OF OXALATE AND CC GLYCOLATE. CC -!- SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56092; CAA39572.1; -. DR EMBL; X53414; CAA37493.1; -. DR EMBL; D13368; BAA02632.1; -. DR EMBL; M61763; AAA51680.1; -. DR PIR; S10557; XNHUSP. DR PIR; A36681; A36681. DR MIM; 604285; -. DR MIM; 259900; -. DR InterPro; IPR000192; Aminotransf_class_V. DR Pfam; PF00266; aminotran_5; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Peroxisome; KW Mitochondrion; Disease mutation; Polymorphism. FT BINDING 209 209 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT VARIANT 11 11 P -> L. FT /FTId=VAR_000587. FT VARIANT 41 41 G -> R (IN PH1). FT /FTId=VAR_000588. FT VARIANT 41 41 G -> V (IN PH1). FT /FTId=VAR_010969. FT VARIANT 82 82 G -> E (IN PH1). FT /FTId=VAR_008878. FT VARIANT 95 95 E -> EE (IN PH1). FT /FTId=VAR_010970. FT VARIANT 116 116 G -> R (IN PH1). FT /FTId=VAR_010971. FT VARIANT 152 152 F -> I (IN PH1). FT /FTId=VAR_000589. FT VARIANT 156 156 G -> R (IN PH1). FT /FTId=VAR_010972. FT VARIANT 170 170 G -> R (IN PH1). FT /FTId=VAR_000590. FT VARIANT 183 183 D -> N (IN PH1). FT /FTId=VAR_010973. FT VARIANT 187 187 S -> F (IN PH1). FT /FTId=VAR_000591. FT VARIANT 205 205 S -> P (IN PH1). FT /FTId=VAR_000592. FT VARIANT 233 233 R -> C (IN PH1). FT /FTId=VAR_008879. FT VARIANT 233 233 R -> H (IN PH1). FT /FTId=VAR_008880. FT VARIANT 244 244 I -> T (IN PH1). FT /FTId=VAR_008881. FT VARIANT 340 340 I -> M. FT /FTId=VAR_000593. SQ SEQUENCE 392 AA; 43010 MW; 2987DDE85B2470B4 CRC64; MASHKLLVTP PKALLKPLSI PNQLLLGPGP SNLPPRIMAA GGLQMIGSMS KDMYQIMDEI KEGIQYVFQT RNPLTLVISG SGHCALEAAL VNVLEPGDSF LVGANGIWGQ RAVDIGERIG ARVHPMTKDP GGHYTLQEVE EGLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL LVDSVASLGG TPLYMDRQGI DILYSGSQKA LNAPPGTSLI SFSDKAKKKM YSRKTKPFSF YLDIKWLANF WGCDDQPRMY HHTIPVISLY SLRESLALIA EQGLENSWRQ HREAAAYLHG RLQALGLQLF VKDPALRLPT VTTVAVPAGY DWRDIVSYVI DHFDIEIMGG LGPSTGKVLR IGLLGCNATR ENVDRVTEAL RAALQHCPKK KL // ID SPYA_MOUSE STANDARD; PRT; 413 AA. AC O35423; DT 20-AUG-2001 (Rel. 40, Created) DT 20-AUG-2001 (Rel. 40, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Serine--pyruvate aminotransferase, mitochondrial precursor DE (EC 2.6.1.51) (SPT) (Alanine--glyoxylate aminotransferase) DE (EC 2.6.1.44) (AGT). GN AGXT OR AGXT1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RA Li X.-M., Salido E.C., Shapiro L.J.; RT "The mouse alanine:glyoxylate aminotransferase gene (Agxt1): cloning, RT expression and mapping to chromosome 1."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DUAL METABOLIC ROLES OF GLUCONEOGENESIS (IN THE CC MITOCHONDRIA) AND GLYOXYLATE DETOXIFICATION (IN THE PEROXISOMES) CC (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: L-SERINE + PYRUVATE = 3-HYDROXYPYRUVATE + CC L-ALANINE. CC -!- CATALYTIC ACTIVITY: L-ALANINE + GLYOXYLATE = PYRUVATE + GLYCINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX AND PEROXISOMES (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF027730; AAB82001.2; -. DR MGD; MGI:1329033; Agxt. DR InterPro; IPR000192; Aminotransf_class_V. DR Pfam; PF00266; aminotran_5; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Peroxisome; KW Mitochondrion; Transit peptide; Alternative initiation. FT TRANSIT 1 23 MITOCHONDRION. FT CHAIN 24 413 SERINE--PYRUVATE AMINOTRANSFERASE, FT MITOCHONDRIAL ISOFORM. FT CHAIN 23 413 SERINE--PYRUVATE AMINOTRANSFERASE, FT PEROXISOMAL ISOFORM. FT INIT_MET 23 23 FOR PEROXISOMAL ISOFORM. FT BINDING 231 231 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT SITE 411 413 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). SQ SEQUENCE 413 AA; 45815 MW; CBAC3DBE68A52504 CRC64; MFRMLAKASV TLGSRAAGWV RTMGSYQLLV PPPEALSKPL SVPTRLLLGP GPSNLAPRVL AAGSLRMIGH MQKEMLQIME EIKQGIQYVF QTRNPLTLVV SGSGHCAMET ALFNLLEPGD SFLTGTNGIW GMRAAEIADR IGARVHQMIK KPGEHYTLQE VEEGLAQHKP VLLFLVHGES STGVVQPLDG FGELCHRYQC LLLVDSVASL GGVPIYMDQQ GIDIMYSSSQ KVLNAPPGIS LISFNDKAKY KVYSRKTKPV SFYTDITYLA KLWGCEGETR VIHHTTPVTS LYCLRESLAL IAERGLENCW RRHREATAHL HKHLQEMGLK FFVKDPEIRL PTITTVTAAG YNWRDIVSYV LDHFSIEISG GLGPTEERVL RIGLLGYNAT TENVDRVAEA LREALQHCPK NKL // ID SPYA_RAT STANDARD; PRT; 414 AA. AC P09139; Q9R2C7; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Serine--pyruvate aminotransferase, mitochondrial precursor DE (EC 2.6.1.51) (SPT) (Alanine--glyoxylate aminotransferase) DE (EC 2.6.1.44) (AGT). GN AGXT OR AGT1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Liver; RX MEDLINE=88029472; PubMed=2822418; RA Oda T., Miyajima H., Suzuki Y., Ichiyama A.; RT "Nucleotide sequence of the cDNA encoding the precursor for RT mitochondrial serine:pyruvate aminotransferase of rat liver."; RL Eur. J. Biochem. 168:537-542(1987). RN [2] RP SEQUENCE OF 1-141 FROM N.A. RC STRAIN=WISTAR; RX MEDLINE=94010910; PubMed=8406472; RA Oda T., Nishiyama K., Ichiyama A.; RT "Characterization and sequence analysis of rat RT serine:pyruvate/alanine:glyoxylate aminotransferase gene."; RL Genomics 17:59-65(1993). RN [3] RP ALTERNATIVE INITIATION. RX MEDLINE=90237053; PubMed=2332438; RA Oda T., Funai T., Ichiyama A.; RT "Generation from a single gene of two mRNAs that encode the RT mitochondrial and peroxisomal serine:pyruvate aminotransferase of rat RT liver."; RL J. Biol. Chem. 265:7513-7519(1990). CC -!- FUNCTION: DUAL METABOLIC ROLES OF GLUCONEOGENESIS (IN THE CC MITOCHONDRIA) AND GLYOXYLATE DETOXIFICATION (IN THE PEROXISOMES). CC -!- CATALYTIC ACTIVITY: L-SERINE + PYRUVATE = 3-HYDROXYPYRUVATE + CC L-ALANINE. CC -!- CATALYTIC ACTIVITY: L-ALANINE + GLYOXYLATE = PYRUVATE + GLYCINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX (INDUCED ON GLUCAGON CC ADMINISTRATION) AND PEROXISOMES (NOT EFFECTED BY GLUCAGON). CC -!- SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06357; CAA29656.1; -. DR EMBL; D13667; BAA02838.1; -. DR EMBL; M35270; AAA42169.1; -. DR PIR; S00164; XNRTSP. DR PIR; A35200; A35200. DR PIR; B35200; B35200. DR InterPro; IPR000192; Aminotransf_class_V. DR Pfam; PF00266; aminotran_5; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. KW Transferase; Aminotransferase; Pyridoxal phosphate; Peroxisome; KW Mitochondrion; Transit peptide; Alternative initiation. FT TRANSIT 1 23 MITOCHONDRION. FT CHAIN 24 414 SERINE--PYRUVATE AMINOTRANSFERASE, FT MITOCHONDRIAL ISOFORM. FT CHAIN 23 414 SERINE--PYRUVATE AMINOTRANSFERASE, FT PEROXISOMAL ISOFORM. FT INIT_MET 23 23 FOR PEROXISOMAL ISOFORM. FT BINDING 231 231 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT SITE 412 414 MICROBODY TARGETING SIGNAL (BY FT SIMILARITY). SQ SEQUENCE 414 AA; 45834 MW; 3FBD66ED36C3D9EF CRC64; MFRMLAKASV TLGSRAASWV RNMGSHQLLV PPPEALSKPL SIPKRLLLGP GPSNLAPRVL AAGSLRMIGH MQKEMFQIMD EIKQGIQYVF QTRNPLTLVV SGSGHCAMET ALFNLLEPGD SFLVGTNGIW GIRAAEIAER IGARVHQMIK KPGEHYTLQE VEEGLAQHKP VLLFLTHGES STGVLQPLDG FGELCHRYQC LLLVDSVASL GGVPIYMDQQ GIDILYSGSQ KVLNAPPGIS LISFNDKAKS KVYSRKTKPV SFYTDITYLS KLWGCEGKTR VIHHTLPVIS LYCLRESLAL ISEQGLENSW RRHREATAHL HKCLRELGLK FFVKDPEIRL PTITTVTVPA GYNWRDIVSY VLDHFNIEIS GGLGPSEDKV LRIGLLGYNA TTENADRVAE ALREALQHCP KNKL