ID ACOX1_YARLI Reviewed; 689 AA. AC O74934; Q6C3Q9; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 51. DE RecName: Full=Acyl-coenzyme A oxidase 1; DE Short=Acyl-CoA oxidase 1; DE EC=1.3.3.6; GN Name=POX1; Synonyms=ACO1; OrderedLocusNames=YALI0E32835g; OS Yarrowia lipolytica (Candida lipolytica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=4952; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29; RA Le Clainche A., Nicaud J.-M.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). RN [3] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX MEDLINE=21686203; PubMed=11815635; DOI=10.1083/jcb.200111075; RA Titorenko V.I., Nicaud J.-M., Wang H., Chan H., Rachubinski R.A.; RT "Acyl-CoA oxidase is imported as a heteropentameric, cofactor- RT containing complex into peroxisomes of Yarrowia lipolytica."; RL J. Cell Biol. 156:481-494(2002). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + CC H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. CC -!- SUBUNIT: Heteropentamer composed of five different subunits. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001299; CAA04659.1; -; Genomic_DNA. DR EMBL; CR382131; CAG80307.1; ALT_INIT; Genomic_DNA. DR RefSeq; XP_504703.1; -. DR HSSP; P07872; 1IS2. DR GeneID; 2912003; -. DR KEGG; yli:YALI0E32835g; -. DR HOGENOM; O74934; -. DR BRENDA; 1.3.3.6; 3602. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006090; Acyl-CoA_Oxase/DH_1. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_M. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR013764; AcylCoA_oxidase/DH_1/2_C. DR Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1. DR Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1. DR Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2. DR PANTHER; PTHR10909:SF11; Acyl-CoA_oxidase; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. PE 1: Evidence at protein level; KW Complete proteome; FAD; Fatty acid metabolism; Flavoprotein; KW Lipid metabolism; Oxidoreductase; Peroxisome. FT CHAIN 1 689 Acyl-coenzyme A oxidase 1. FT /FTId=PRO_0000204701. FT ACT_SITE 444 444 Proton acceptor (By similarity). FT BINDING 149 149 FAD (By similarity). FT BINDING 188 188 FAD; via amide nitrogen (By similarity). SQ SEQUENCE 689 AA; 77282 MW; 843D99D6DCEB4150 CRC64; MTTNTFTDPP VEMAKERGKT QFTVRDVTNF LNGGEEETQI VEKIMSSIER DPVLSVTADY DCNLQQARKQ TMERVAALSP YLVTDTEKLS LWRAQLHGMV DMSTRTRLSI HNNLFIGSIR GSGTPEQFKY WVKKGAVAVK QFYGCFAMTE LGHGSNLKGL ETTATYDQDS DQFIINTPHI GATKWWIGGA AHTSTHCVCF AKLIVHGKDY GTRNFVVPLR NVHDHSLKVG VSIGDIGKKM GRDGVDNGWI QFTNVRIPRQ NMLMRYAKVS DTGVVTKPAL DQLTYGALIR GRVSMIADSF HVSKRFLTIA LRYACVRRQF GTSGDTKETK IIDYPYHQRR LLPLLAYCYA MKMGADEAQK TWIETTDRIL ALNPNDPAQK NDLEKAVTDT KELFAASAGM KAFTTWGCAK IIDECRQACG GHGYSGYNGF GQGYADWVVQ CTWEGDNNVL CLSMGRGLVQ SALQILAGKH VGASIQYVGD KSKISQNGQG TPREQLLSPE FLVEAFRTAS RNNILRTTDK YQELVKTLNP DQAFEELSQQ RFQCARIHTR QHLISSFYAR IATAKDDIKP HLLKLANLFA LWSIEEDTGI FLRENILTPG DIDLINSLVD ELCVAVRDQV IGLTDAFGLS DFFINAPIGS YDGNVYEKYF AKVNQQNPAT NPRPPYYEST LKPFLFREEE DDEICDLDE //