ID A0A7K6XL06_9PASE Unreviewed; 666 AA. AC A0A7K6XL06; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 27-MAR-2024, entry version 11. DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000256|ARBA:ARBA00040310}; DE EC=1.3.3.6 {ECO:0000256|ARBA:ARBA00012870}; DE AltName: Full=Palmitoyl-CoA oxidase {ECO:0000256|ARBA:ARBA00041259}; DE AltName: Full=Peroxisomal fatty acyl-CoA oxidase {ECO:0000256|ARBA:ARBA00042468}; DE AltName: Full=Straight-chain acyl-CoA oxidase {ECO:0000256|ARBA:ARBA00041501}; DE Flags: Fragment; GN Name=Acox1 {ECO:0000313|EMBL:NWX59998.1}; GN ORFNames=PROCAF_R03364 {ECO:0000313|EMBL:NWX59998.1}; OS Promerops cafer (Cape sugarbird). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Nectariniidae; OC Promerops. OX NCBI_TaxID=254652 {ECO:0000313|EMBL:NWX59998.1, ECO:0000313|Proteomes:UP000587587}; RN [1] {ECO:0000313|EMBL:NWX59998.1, ECO:0000313|Proteomes:UP000587587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-UC-030-53 {ECO:0000313|EMBL:NWX59998.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + O2 = CC (2E,5Z,8Z,11Z,14Z,17Z)-icosahexaenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:69643, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:73862, ChEBI:CHEBI:187901; CC Evidence={ECO:0000256|ARBA:ARBA00036444}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69644; CC Evidence={ECO:0000256|ARBA:ARBA00036444}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + O2 = CC (2E,6Z,9Z,12Z,15Z,18Z,21Z)-tetracosaheptaenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:39119, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:74086, ChEBI:CHEBI:76360; CC Evidence={ECO:0000256|ARBA:ARBA00036338}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39120; CC Evidence={ECO:0000256|ARBA:ARBA00036338}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + octadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:38971, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57394, ChEBI:CHEBI:71412; CC Evidence={ECO:0000256|ARBA:ARBA00036774}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972; CC Evidence={ECO:0000256|ARBA:ARBA00036774}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + octanoyl-CoA = (2E)-octenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40175, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62242; CC Evidence={ECO:0000256|ARBA:ARBA00036210}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176; CC Evidence={ECO:0000256|ARBA:ARBA00036210}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40319, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; CC Evidence={ECO:0000256|ARBA:ARBA00036229}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320; CC Evidence={ECO:0000256|ARBA:ARBA00036229}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40183, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57385, ChEBI:CHEBI:61405; CC Evidence={ECO:0000256|ARBA:ARBA00036028}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184; CC Evidence={ECO:0000256|ARBA:ARBA00036028}; 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:ARBA00036397}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; CC Evidence={ECO:0000256|ARBA:ARBA00036397}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanoyl-CoA + O2 = (2E)-decenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40179, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430; CC Evidence={ECO:0000256|ARBA:ARBA00036151}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180; CC Evidence={ECO:0000256|ARBA:ARBA00036151}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40171, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57330, ChEBI:CHEBI:57375; CC Evidence={ECO:0000256|ARBA:ARBA00036791}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172; CC Evidence={ECO:0000256|ARBA:ARBA00036791}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glutaryl-CoA + O2 = (2E)-glutaconyl-CoA + H2O2; CC Xref=Rhea:RHEA:40315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57353, ChEBI:CHEBI:57378; CC Evidence={ECO:0000256|ARBA:ARBA00036750}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40316; CC Evidence={ECO:0000256|ARBA:ARBA00036750}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanedioyl-CoA + O2 = (2E)-hexadecenedioyl-CoA + H2O2; CC Xref=Rhea:RHEA:40275, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:77075, ChEBI:CHEBI:77085; CC Evidence={ECO:0000256|ARBA:ARBA00036704}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276; CC Evidence={ECO:0000256|ARBA:ARBA00036704}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:61526; CC Evidence={ECO:0000256|ARBA:ARBA00036893}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168; CC Evidence={ECO:0000256|ARBA:ARBA00036893}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexanoyl-CoA + O2 = (2E)-hexenoyl-CoA + H2O2; CC Xref=Rhea:RHEA:40311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; CC Evidence={ECO:0000256|ARBA:ARBA00036399}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312; CC Evidence={ECO:0000256|ARBA:ARBA00036399}; 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NWX59998.1}. 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; VZSE01007656; NWX59998.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7K6XL06; -. DR Proteomes; UP000587587; Unassembled WGS sequence. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0005504; F:fatty acid binding; IEA:InterPro. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:InterPro. DR CDD; cd01150; AXO; 1. 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; IPR034171; ACO. 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; 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:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 1. DR Pfam; PF01756; ACOX; 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|PIRSR:PIRSR000168-2}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000587587}. FT DOMAIN 21..138 FT /note="Acyl-coenzyme A oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF14749" FT DOMAIN 141..249 FT /note="Acyl-CoA oxidase/dehydrogenase middle" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 484..662 FT /note="Acyl-CoA oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF01756" FT ACT_SITE 426 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1" FT BINDING 144 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2" FT BINDING 183 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NWX59998.1" FT NON_TER 666 FT /evidence="ECO:0000313|EMBL:NWX59998.1" SQ SEQUENCE 666 AA; 74726 MW; 587BD221E522595C CRC64; AAAMSVNADL RRERAAASFQ PELLTHILDG GPERTRRRKE IEALVLNDPD FQHEDLNFLS RSQRYEQAIR KSSLMVMKLR EYGIADPEEI YWFKSFVHRG RPEPLDLHLG MFLPTLLTQA TPEQQDRFFM PAWNLEIIGT YAQTEMGHGT HLRGLETTAT YDPSTQEFIL NSPTVTSIKW WPGGLGKTSN HAIVLAQLYT QGQCKGLHAF IVPIRQLGTH EPLPGITVGD IGPKFGYDEM DNGYLKMDNF RIPRENMLMK YAQVEPDGTY VKPVSDKLTY GTMVFIRSLI VGDSARSLSR ACTIAIRYSA VRHQSELKPG EPEPQILDYQ TQQYKLFPLL ATAYAFHFVG AYIKDTYHRI SGDISTGDLT ELPELHALTA GLKAFTSWTA NAGIEECRMA CGGHGYSRCS GIPDIYVTFT PSCTYEGENT VMMLQTARFL IKSYTQVTSG QQVTGMVSYL NDVSRQRIQP QHVAARTVTV RISDPTSLVE AYKSRAARLV ESAAKNLQAE LNHRKSKEDA WNRTSVDLVR ASEAHCHYVI VKLFTAKLAE VSDGAVRAVL TDLCLLYALF GISRNAGDFL QAGILTSAQI TQVNQHVKEL LAVIRPNAVA LVDSFDFHDV HLGSVLGRYD GNVYENMFEW AKKSPLNKSQ VHESFHKHLK PMQAKL //