ID B9WDG7_CANDC Unreviewed; 709 AA. AC B9WDG7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168}; GN Name=POX1 {ECO:0000313|EMBL:CAX42723.1}; GN OrderedLocusNames=Cd36_81950 {ECO:0000313|CGD:CAL0000164518}; GN ORFNames=CD36_81950 {ECO:0000313|EMBL:CAX42723.1}; OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / OS NRRL Y-17841) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX42723.1, ECO:0000313|Proteomes:UP000002605}; RN [1] {ECO:0000313|EMBL:CAX42723.1, ECO:0000313|Proteomes:UP000002605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841 RC {ECO:0000313|Proteomes:UP000002605}; RX PubMed=19745113; DOI=10.1101/gr.097501.109; RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D., RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C., RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A., RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J., RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.; RT "Comparative genomics of the fungal pathogens Candida dubliniensis and RT Candida albicans."; RL Genome Res. 19:2231-2244(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; CC Evidence={ECO:0000256|ARBA:ARBA00001201}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. CC {ECO:0000256|ARBA:ARBA00004846}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}. CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FM992690; CAX42723.1; -; Genomic_DNA. DR RefSeq; XP_002419134.1; XM_002419089.1. DR AlphaFoldDB; B9WDG7; -. DR GeneID; 8047077; -. DR KEGG; cdu:CD36_81950; -. DR CGD; CAL0000164518; Cd36_81950. DR VEuPathDB; FungiDB:CD36_81950; -. DR eggNOG; KOG0136; Eukaryota. DR HOGENOM; CLU_014629_3_1_1; -. DR OrthoDB; 5777at2759; -. DR UniPathway; UPA00661; -. DR Proteomes; UP000002605; Chromosome 3. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2. DR InterPro; IPR029320; Acyl-CoA_ox_N. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR012258; Acyl-CoA_oxidase. DR InterPro; IPR002655; Acyl-CoA_oxidase_C. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1. DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 1. DR Pfam; PF01756; ACOX; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF14749; Acyl-CoA_ox_N; 1. DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000168}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|PIRNR:PIRNR000168}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Oxidoreductase {ECO:0000313|EMBL:CAX42723.1}; KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}. FT DOMAIN 30..144 FT /note="Acyl-coenzyme A oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF14749" FT DOMAIN 154..263 FT /note="Acyl-CoA oxidase/dehydrogenase middle" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 408..468 FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00441" FT DOMAIN 515..687 FT /note="Acyl-CoA oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF01756" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 456 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1" FT BINDING 158 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2" FT BINDING 197 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2" SQ SEQUENCE 709 AA; 78790 MW; 73C6FDDD66D63EBB CRC64; MSFTKKNVSL AQGPDPRSSI QTERANSKFN PEKMNYFLEG SKERSELFKG LAQQMERDPV LFTDGSYYDL TKDQQRELTA VKINRLARYR ETDSIDTFNK RLSLVGVFDP QVGTRIGVNL GLFLSCIRGN GTAEQLKYWA FDKETSNIKG IYGCFGMTEL AHGSNVAGLE TTATFDKEND EFVINTPHVG ATKWWIGGAA HSATHCSVYA RLIVDGEDYG VKTFVVPLRD SNHDLMPGVT VGDIGAKMGR DGIDNGWIQF SNVRIPRFFM LQKFCKVSAD GEVVLPPLEQ LSYSALLGGR VMMVLDSYRM LARMSTIALR YAIGRRQFKG DNVDQNDPNA LETQLIDYPL HQKRLFPYLA AAYVISAGAL KIEHTIETTL EELDQAVAKG DQRAIFKSID DMKSLFVDSG SLKSTATWLA AEAIDQCRQA CGGHGYSSYN GFGKAYNDWV VQCTWEGDNN VLGMSVGKPI VREVINLEDK GKKVRGSTAF LNQLKEYTGS NSSKVVLDSV ADLDDVNKVI KAIEVAIIRL AQEAATTVRK ESLDFVGAEL VQLSKLKAHH YSLTEYVRRV NEFDQKDLVP YLLTIAKLYG ATVVLDKFAG VFLTFNVAST KAITDLASVQ IPKLCAEVRP NVVAYTDSFQ QSDMIVNSAI GRYDGDIYEN YFDLVKAQNP PSKTKAPYSA ALEAMLNRPS LEARERFEKT DETAEILSK //