ACOX3_PONAB
ID ACOX3_PONAB Reviewed; 700 AA.
AC Q5RAU0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 3;
DE EC=1.3.3.6 {ECO:0000250|UniProtKB:Q63448};
DE AltName: Full=Branched-chain acyl-CoA oxidase;
DE Short=BRCACox;
DE AltName: Full=Pristanoyl-CoA oxidase {ECO:0000250|UniProtKB:Q63448};
GN Name=ACOX3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids.
CC {ECO:0000250|UniProtKB:Q63448}.
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:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-pristanoyl-CoA + O2 = (2E)-pristenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40459, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:77099, ChEBI:CHEBI:77293;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40460;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
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:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
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:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
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:0000250|UniProtKB:Q63448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000250|UniProtKB:Q63448};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P07872};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; CR858922; CAH91120.1; -; mRNA.
DR RefSeq; NP_001125655.1; NM_001132183.1.
DR AlphaFoldDB; Q5RAU0; -.
DR SMR; Q5RAU0; -.
DR STRING; 9601.ENSPPYP00000016272; -.
DR PRIDE; Q5RAU0; -.
DR GeneID; 100172575; -.
DR KEGG; pon:100172575; -.
DR CTD; 8310; -.
DR eggNOG; KOG0135; Eukaryota.
DR InParanoid; Q5RAU0; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IEA:InterPro.
DR GO; GO:0016402; F:pristanoyl-CoA oxidase activity; IEA:RHEA.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR034171; ACO.
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; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR PANTHER; PTHR10909; PTHR10909; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 2: Evidence at transcript level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15254"
FT CHAIN 2..700
FT /note="Peroxisomal acyl-coenzyme A oxidase 3"
FT /id="PRO_0000290353"
FT MOTIF 698..700
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q63448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15254"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15254"
SQ SEQUENCE 700 AA; 77865 MW; C405A0D65A2796E5 CRC64;
MASTVEGGDT ALLPEFPGGP LDAYRARASF SWKELALFTE GEDMLRFKKT IFSALENDPL
FARSPGADLS LEKYRELNFL RCRRIFEYDF LSVEDMFKSP LKVLTLIQCL GMYDSSLAAK
YLIHSLVFGS AIYSSGSERH LTYIQKIFRM EIFGCFALTE LSHGSNTKAI RTTAHYDPAT
EEFIIHSPDF EAAKFWVGNM GKTATHAVVF AKLYVPGDQC HGLHPFIVQI RDSKTLLPMP
GVMVGDIGKK LGQNGLDNGF AMFHKVRVPR QSLLNRMGDV TPEGTYVSSF KDVRQHFGAT
LGSLSWSRVS IVSLAILNLK LAVAIALRFS ATRRQFGPTE EEEIPVLEYP MQQWRLLPYL
AAIYALDHFS KSLFLDLMEL QQGLASGDRS ARQAELGREI HALASASKPL ASWTTQQGIQ
ECREACGGHG YLAMNRLGVL RDDNDPNCTY EGDNNILLQQ TSNYLLGLLA HQVQDGACFR
SPLKSVDFLD AYPGILDQKF EVSSVADCLD SAVALAAYKW LVCYLLRETY QKLNQEKRSG
SSDFEARNKC QVSHGRPLAL AFVELTVVQR FHEHVHQPCV PPSLRAVLGR LSALYALWSL
SRHAALLYRG GYFSGEQAGE VLESAVLALC SQLKDDAVAL VDVIAPPDFI LDSPIGRADG
ELYKNLWGAI LQESKALERA SWWPEFSVNK PVIGSLKSKL
