ACOX1_BOVIN
ID ACOX1_BOVIN Reviewed; 660 AA.
AC Q3SZP5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Peroxisomal acyl-coenzyme A oxidase 1 {ECO:0000250|UniProtKB:Q15067};
DE Short=AOX {ECO:0000250|UniProtKB:Q15067};
DE EC=1.3.3.6 {ECO:0000250|UniProtKB:P07872};
DE AltName: Full=Palmitoyl-CoA oxidase {ECO:0000250|UniProtKB:Q15067};
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:0000250|UniProtKB:P07872};
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, B chain {ECO:0000250|UniProtKB:P07872};
DE Contains:
DE RecName: Full=Peroxisomal acyl-CoA oxidase 1, C chain {ECO:0000250|UniProtKB:P07872};
GN Name=ACOX1 {ECO:0000250|UniProtKB:Q15067};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q15067}.
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:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960;
CC Evidence={ECO:0000250|UniProtKB:P07872};
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:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40168;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40172;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40176;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40180;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:0000250|UniProtKB:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40184;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:Q15067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40276;
CC Evidence={ECO:0000250|UniProtKB:Q15067};
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:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40320;
CC Evidence={ECO:0000250|UniProtKB:P07872};
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:0000250|UniProtKB:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40316;
CC Evidence={ECO:0000250|UniProtKB:P07872};
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:0000250|UniProtKB:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40312;
CC Evidence={ECO:0000250|UniProtKB:P07872};
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:0000250|UniProtKB:P07872};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38972;
CC Evidence={ECO:0000250|UniProtKB:P07872};
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:0000250|UniProtKB:P07872};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with LONP2 (By
CC similarity). {ECO:0000250|UniProtKB:P07872,
CC ECO:0000250|UniProtKB:Q15067}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P07872}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR EMBL; BC102761; AAI02762.1; -; mRNA.
DR RefSeq; NP_001030366.1; NM_001035289.3.
DR AlphaFoldDB; Q3SZP5; -.
DR SMR; Q3SZP5; -.
DR STRING; 9913.ENSBTAP00000029362; -.
DR PaxDb; Q3SZP5; -.
DR PeptideAtlas; Q3SZP5; -.
DR PRIDE; Q3SZP5; -.
DR Ensembl; ENSBTAT00000029362; ENSBTAP00000029362; ENSBTAG00000030174.
DR GeneID; 513996; -.
DR KEGG; bta:513996; -.
DR CTD; 51; -.
DR VEuPathDB; HostDB:ENSBTAG00000030174; -.
DR VGNC; VGNC:25552; ACOX1.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000157287; -.
DR InParanoid; Q3SZP5; -.
DR OMA; TKWWIGA; -.
DR OrthoDB; 416859at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030174; Expressed in adult mammalian kidney and 111 other tissues.
DR ExpressionAtlas; Q3SZP5; baseline and differential.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; ISS:UniProtKB.
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:0140493; P:very long-chain fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..660
FT /note="Peroxisomal acyl-CoA oxidase 1, A chain"
FT /id="PRO_0000281996"
FT CHAIN 1..438
FT /note="Peroxisomal acyl-CoA oxidase 1, B chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447496"
FT CHAIN 439..660
FT /note="Peroxisomal acyl-CoA oxidase 1, C chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447497"
FT MOTIF 658..660
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT BINDING 178
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT SITE 468..469
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P07872"
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 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 651
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
FT MOD_RES 654
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0H0"
SQ SEQUENCE 660 AA; 74379 MW; 606F86A63915DF9D CRC64;
MNPDLQKERA GASFNPELLT NVLDGSPENT RRRREIENLI LNDPDFQHEN LNFLSRSQRY
EVAVKKSAIM VQKMRKFGIA DPAEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQQ
EKWLHSSKGL EIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL
GKTSNHAIVL AQLFTQGKCY GLHAFIVPIR ELGTHKPLPG ITVGDIGPKF GYDEMDNGYL
KMDNYRIPRE NMLMKHAQVK PDGTYVKPLN NKLTYGTMVF IRSFLVGESA RSLSKACTIA
VRYSAVRHQS EINPGEPEPQ ILDYQTQQYK LFPLLATAYA FQFVGAYMKE TYLRINEDIG
HGDLSELPEL HALTAGLKAF TSWTTNTAIE ACRMACGGHG YSHCSGLPNI YVTFTPTCTF
EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP
DSLTEAYKLR AARLVEIAAK NLQTEVIHRK SKEVAWNLTS IDLVRASEAH CHYVVVKLFT
EKVLQIQEKS IQAVLRRLCL LYSLYGISQN AGDFLQGSIM TESQITQVNG RIKELLTAIR
PDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY KHLKSLQSKL
