ACOX1_CAVPO
ID ACOX1_CAVPO Reviewed; 661 AA.
AC Q9Z1N0;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
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:0000303|Ref.1};
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};
GN Synonyms=PCOX1 {ECO:0000303|Ref.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Baumgart E., Van Veldhoven P.P., Althoff B., Mannaerts G.P., Voelkl A.,
RA Fahimi D.;
RT "Molecular characterization of guinea pig peroxisomal palmitoyl-CoA oxidase
RT 1.";
RL Submitted (APR-1998) 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; AJ005112; CAA06376.1; -; mRNA.
DR RefSeq; NP_001166377.1; NM_001172906.1.
DR AlphaFoldDB; Q9Z1N0; -.
DR SMR; Q9Z1N0; -.
DR STRING; 10141.ENSCPOP00000014695; -.
DR GeneID; 100135467; -.
DR KEGG; cpoc:100135467; -.
DR CTD; 51; -.
DR eggNOG; KOG0136; Eukaryota.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; Q9Z1N0; -.
DR OrthoDB; 416859at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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; IEA:InterPro.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
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:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
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..661
FT /note="Peroxisomal acyl-CoA oxidase 1, A chain"
FT /id="PRO_0000204676"
FT CHAIN 1..438
FT /note="Peroxisomal acyl-CoA oxidase 1, B chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447498"
FT CHAIN 439..661
FT /note="Peroxisomal acyl-CoA oxidase 1, C chain"
FT /evidence="ECO:0000250|UniProtKB:P07872"
FT /id="PRO_0000447499"
FT MOTIF 659..661
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 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"
SQ SEQUENCE 661 AA; 74390 MW; D360D9515259E76A CRC64;
MNPDLRRERA AATFNPELIT HLLDGSPEKT RRRREIENKI LSDPDFQHEN HNFLTRSERY
EAAIKKSAVM VKKMREFGIA DPDEIMWFKR LLLGNFVEPV GLNYSMFIPT LLNQGTTAQQ
EKWLHPSTGL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFIINSPTV TSIKWWPGGL
GKTSNHAIVL AQLITQGKCY GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL
KMDNYRIPRE NMLMKYAQVK PDGTYVKPVS NKLTYGTMVF VRSFLVGAAA QSLSKACTIA
IRYSAVRHQS EIKPGEPEPQ VLDFQTQQYK LFPILATAYA FQFVGSYMKD TYHRINESIG
QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRLACGGHG YSHCSGIPNI YVTFTPACTF
EGENTVMMLQ TARFLMKVYD QVQSGKLVHG LVSYLNDLPS QRIQPQQVAV WPTVVDINNP
DSLTEIYKLR AARLIDIAAK SLQGEMSHRK SKEVAWNLTS VGLVRATDAH CHYVVVKLFA
DKLLKIQDKT IQAVLRNLFL LYSLYGISQK AGDFLQGNIM TGSQITQVNQ RVLELLAVIR
PNAVALVDAF DYKDITLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY HKYLKPLQSK
L
