ACOX1_RAT
ID ACOX1_RAT Reviewed; 661 AA.
AC P07872; P11354;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000303|PubMed:11872165, ECO:0000303|PubMed:16672280, ECO:0000303|PubMed:7503725};
DE Short=ACO {ECO:0000303|PubMed:11872165, ECO:0000303|PubMed:16672280, ECO:0000303|PubMed:7503725};
DE Short=AOX {ECO:0000250|UniProtKB:Q15067};
DE EC=1.3.3.6 {ECO:0000269|PubMed:16672280, ECO:0000269|PubMed:7503725, ECO:0000305|PubMed:1400324, ECO:0000305|PubMed:7462191};
DE AltName: Full=Palmitoyl-CoA oxidase {ECO:0000303|PubMed:1400324};
DE AltName: Full=Peroxisomal fatty acyl-CoA oxidase;
DE AltName: Full=Straight-chain acyl-CoA oxidase;
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, A chain {ECO:0000303|PubMed:3036800};
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, B chain {ECO:0000303|PubMed:3036800};
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, C chain {ECO:0000303|PubMed:3036800};
GN Name=Acox1 {ECO:0000312|RGD:619757};
GN Synonyms=Acox {ECO:0000303|PubMed:15489334};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 469-491,
RP AND CLEAVAGE SITE.
RX PubMed=3036800; DOI=10.1016/s0021-9258(18)47539-4;
RA Miyazawa S., Hayashi H., Hijikata M., Ishii N., Furuta S., Kagamiyama H.,
RA Osumi T., Hashimoto T.;
RT "Complete nucleotide sequence of cDNA and predicted amino acid sequence of
RT rat acyl-CoA oxidase.";
RL J. Biol. Chem. 262:8131-8137(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Brown Norway; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=3036801; DOI=10.1016/s0021-9258(18)47540-0;
RA Osumi T., Ishii N., Miyazawa S., Hashimoto T.;
RT "Isolation and structural characterization of the rat acyl-CoA oxidase
RT gene.";
RL J. Biol. Chem. 262:8138-8143(1987).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7462191; DOI=10.1093/oxfordjournals.jbchem.a133118;
RA Kawaguchi A., Tsubotani S., Seyama Y., Yamakawa T., Osumi T., Hashimoto T.,
RA Kikuchi T., Ando M., Okuda S.;
RT "Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase.";
RL J. Biochem. 88:1481-1486(1980).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=1400324; DOI=10.1016/s0021-9258(19)88666-0;
RA Van Veldhoven P.P., Vanhove G., Assselberghs S., Eyssen H.J.,
RA Mannaerts G.P.;
RT "Substrate specificities of rat liver peroxisomal acyl-CoA oxidases:
RT palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase
RT (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase.";
RL J. Biol. Chem. 267:20065-20074(1992).
RN [6]
RP CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), AND FUNCTION (ISOFORMS 1 AND 2).
RX PubMed=7503725; DOI=10.1006/bbrc.1995.2801;
RA Setoyama C., Tamaoki H., Nishina Y., Shiga K., Miura R.;
RT "Functional expression of two forms of rat acyl-CoA oxidase and their
RT substrate specificities.";
RL Biochem. Biophys. Res. Commun. 217:482-487(1995).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=32169171; DOI=10.1016/j.neuron.2020.02.021;
RG Members of Undiagnosed Diseases Network;
RA Chung H.L., Wangler M.F., Marcogliese P.C., Jo J., Ravenscroft T.A.,
RA Zuo Z., Duraine L., Sadeghzadeh S., Li-Kroeger D., Schmidt R.E.,
RA Pestronk A., Rosenfeld J.A., Burrage L., Herndon M.J., Chen S.,
RA Shillington A., Vawter-Lee M., Hopkin R., Rodriguez-Smith J.,
RA Henrickson M., Lee B., Moser A.B., Jones R.O., Watkins P., Yoo T., Mar S.,
RA Choi M., Bucelli R.C., Yamamoto S., Lee H.K., Prada C.E., Chae J.H.,
RA Vogel T.P., Bellen H.J.;
RT "Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Loss via
RT Different Mechanisms.";
RL Neuron 106:589.e6-606.e6(2020).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH A C12-FATTY ACID
RP (ISOFORM 2), SUBUNIT, ACTIVE SITE, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=11872165; DOI=10.1093/oxfordjournals.jbchem.a003111;
RA Nakajima Y., Miyahara I., Hirotsu K., Nishina Y., Shiga K., Setoyama C.,
RA Tamaoki H., Miura R.;
RT "Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from
RT rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA
RT dehydrogenase.";
RL J. Biochem. 131:365-374(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS)(ISOFORM 2), FUNCTION, SUBUNIT,
RP CATALYTIC ACTIVITY (ISOFORM 2), ACTIVE SITE, AND COFACTOR.
RX PubMed=16672280; DOI=10.1093/jb/mvj088;
RA Tokuoka K., Nakajima Y., Hirotsu K., Miyahara I., Nishina Y., Shiga K.,
RA Tamaoki H., Setoyama C., Tojo H., Miura R.;
RT "Three-dimensional structure of rat-liver acyl-CoA oxidase in complex with
RT a fatty acid: insights into substrate-recognition and reactivity toward
RT molecular oxygen.";
RL J. Biochem. 139:789-795(2006).
CC -!- FUNCTION: Involved in the initial and rate-limiting step of peroxisomal
CC beta-oxidation of straight-chain saturated and unsaturated very-long-
CC chain fatty acids. Catalyzes the desaturation of fatty acyl-CoAs such
CC as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-
CC CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to
CC molecular oxygen (O(2)), thereby producing hydrogen peroxide
CC (H(2)O(2)). {ECO:0000269|PubMed:1400324, ECO:0000269|PubMed:16672280,
CC ECO:0000269|PubMed:7462191, ECO:0000269|PubMed:7503725}.
CC -!- FUNCTION: [Isoform 1]: Shows highest activity against medium-chain
CC fatty acyl-CoAs. Shows optimum activity with a chain length of 10
CC carbons (decanoyl-CoA) in vitro. {ECO:0000269|PubMed:7503725}.
CC -!- FUNCTION: [Isoform 2]: Is active against a much broader range of
CC substrates and shows activity towards long-chain acyl-CoAs.
CC {ECO:0000269|PubMed:7503725}.
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:0000269|PubMed:16672280, ECO:0000269|PubMed:7503725,
CC ECO:0000305|PubMed:1400324, ECO:0000305|PubMed:7462191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000305|PubMed:11872165, ECO:0000305|PubMed:1400324,
CC ECO:0000305|PubMed:16672280, ECO:0000305|PubMed:7462191,
CC ECO:0000305|PubMed:7503725};
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:0000305|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:1400324};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172;
CC Evidence={ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:16672280, ECO:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172;
CC Evidence={ECO:0000305|PubMed:16672280, ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176;
CC Evidence={ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180;
CC Evidence={ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184;
CC Evidence={ECO:0000305|PubMed:7503725};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184;
CC Evidence={ECO:0000305|PubMed:7503725};
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:0000305|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000305|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000305|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40316;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000305|PubMed:1400324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312;
CC Evidence={ECO:0000305|PubMed:1400324};
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:0000305|PubMed:7462191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972;
CC Evidence={ECO:0000305|PubMed:7462191};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:0000269|PubMed:7503725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972;
CC Evidence={ECO:0000305|PubMed:7503725};
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:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69644;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:0000250|UniProtKB:Q9R0H0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39120;
CC Evidence={ECO:0000250|UniProtKB:Q9R0H0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11872165, ECO:0000269|PubMed:16672280};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBUNIT: Homodimer. The enzyme contains three components A, B and C,
CC the latter two being produced from the first by a proteolytic cleavage.
CC Interacts with LONP2 (By similarity). {ECO:0000250|UniProtKB:Q15067,
CC ECO:0000269|PubMed:11872165, ECO:0000269|PubMed:16672280}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11872165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ACO-I;
CC IsoId=P07872-1; Sequence=Displayed;
CC Name=2; Synonyms=ACO-II;
CC IsoId=P07872-2; Sequence=VSP_000147;
CC -!- TISSUE SPECIFICITY: Expressed in Schwann cells (PubMed:32169171).
CC Expressed (at protein level) in liver (PubMed:1400324).
CC {ECO:0000269|PubMed:1400324, ECO:0000269|PubMed:32169171}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; J02752; AAA40666.1; -; mRNA.
DR EMBL; BC085743; AAH85743.1; -; mRNA.
DR EMBL; J02753; AAA40667.1; -; Genomic_DNA.
DR PIR; A29328; OXRTA1.
DR PIR; B29328; OXRTA2.
DR RefSeq; NP_059036.1; NM_017340.2. [P07872-1]
DR PDB; 1IS2; X-ray; 2.20 A; A/B=1-661.
DR PDB; 2DDH; X-ray; 2.07 A; A=1-661.
DR PDBsum; 1IS2; -.
DR PDBsum; 2DDH; -.
DR AlphaFoldDB; P07872; -.
DR SMR; P07872; -.
DR IntAct; P07872; 7.
DR STRING; 10116.ENSRNOP00000051538; -.
DR BindingDB; P07872; -.
DR ChEMBL; CHEMBL4632; -.
DR SwissLipids; SLP:000000408; -.
DR CarbonylDB; P07872; -.
DR iPTMnet; P07872; -.
DR PhosphoSitePlus; P07872; -.
DR jPOST; P07872; -.
DR PaxDb; P07872; -.
DR PRIDE; P07872; -.
DR Ensembl; ENSRNOT00000042372; ENSRNOP00000051538; ENSRNOG00000008755. [P07872-1]
DR Ensembl; ENSRNOT00000046754; ENSRNOP00000042132; ENSRNOG00000008755. [P07872-2]
DR GeneID; 50681; -.
DR KEGG; rno:50681; -.
DR CTD; 51; -.
DR RGD; 619757; Acox1.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000157287; -.
DR InParanoid; P07872; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; P07872; -.
DR BRENDA; 1.3.3.6; 5301.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; P07872; -.
DR UniPathway; UPA00661; -.
DR EvolutionaryTrace; P07872; -.
DR PRO; PR:P07872; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IDA:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IDA:RGD.
DR GO; GO:0009062; P:fatty acid catabolic process; ISO:RGD.
DR GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0140493; P:very long-chain fatty acid beta-oxidation; ISO:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
DR CDD; cd01150; AXO; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
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.
DR PANTHER; PTHR10909; PTHR10909; 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; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..661
FT /note="Peroxisomal acyl-CoA oxidase 1, A chain"
FT /id="PRO_0000000552"
FT CHAIN 1..468
FT /note="Peroxisomal acyl-CoA oxidase 1, B chain"
FT /evidence="ECO:0000305|PubMed:3036800"
FT /id="PRO_0000000553"
FT CHAIN 469..661
FT /note="Peroxisomal acyl-CoA oxidase 1, C chain"
FT /evidence="ECO:0000305|PubMed:3036800"
FT /id="PRO_0000000554"
FT MOTIF 659..661
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11872165,
FT ECO:0000269|PubMed:16672280"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11872165,
FT ECO:0000269|PubMed:16672280"
FT BINDING 178
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11872165,
FT ECO:0000269|PubMed:16672280"
FT SITE 468..469
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:3036800"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 89
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 159
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 241
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 255
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 349
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 437
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 437
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 446
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 446
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15067"
FT MOD_RES 512
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 512
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 542
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 637
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 637
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 643
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 652
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 655
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT VAR_SEQ 90..133
FT /note="KLYLANFVEPVGLNYSMFIPTLLNQGTTAQQEKWMRPSQELQII -> NSVH
FT RGHPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3036800"
FT /id="VSP_000147"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 56..76
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2DDH"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:2DDH"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1IS2"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2DDH"
FT TURN 178..183
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:2DDH"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:1IS2"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 279..306
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 325..353
FT /evidence="ECO:0007829|PDB:2DDH"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:1IS2"
FT HELIX 367..395
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 424..444
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 480..509
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 512..518
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 520..542
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 549..569
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 571..576
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 582..599
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 603..608
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 628..638
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:2DDH"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:2DDH"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:2DDH"
SQ SEQUENCE 661 AA; 74679 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
