ID A8X5F5_CAEBR Unreviewed; 655 AA.
AC A8X5F5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=CBG07946 {ECO:0000313|EMBL:CAP27866.1,
GN ECO:0000313|WormBase:CBG07946}, CBG_07946
GN {ECO:0000313|EMBL:CAP27866.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP27866.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP27866.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP27866.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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, ECO:0000256|PIRNR:PIRNR000168}.
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DR EMBL; HE600996; CAP27866.1; -; Genomic_DNA.
DR RefSeq; XP_002646080.1; XM_002646034.1.
DR AlphaFoldDB; A8X5F5; -.
DR STRING; 6238.A8X5F5; -.
DR EnsemblMetazoa; CBG07946.1; CBG07946.1; WBGene00029833.
DR GeneID; 8588132; -.
DR KEGG; cbr:CBG_07946; -.
DR CTD; 8588132; -.
DR WormBase; CBG07946; CBP07788; WBGene00029833; -.
DR eggNOG; KOG0136; Eukaryota.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; A8X5F5; -.
DR OMA; CIIARNM; -.
DR OrthoDB; 5777at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:1904070; P:ascaroside biosynthetic process; IBA:GO_Central.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
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; IPR029320; Acyl-CoA_ox_N.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549}.
FT DOMAIN 17..137
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 474..650
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 655 AA; 73987 MW; D2169DC263804A6D CRC64;
MSENPDLTNE RASGTFDTNA MAAVIYGSEK FAQRRREITE AISKIPEFQD SHPLVFMSRE
EKISEACRKL AVLSNYWNSL IDTSDEEEAL HLYREVLGLE GHPLALHETM FIPSLIAQAS
DEQQEKWLGR AQRREIIGCY AQTEMGHGTN LRALETTATF DISTREFILN SPTITSLKWW
PGALGKSANW SIVIANLIIK EHNYGPHPFM VQLRDEKSHE PLPGITVGDI GPKMAFNGAD
NGFLGFKNYR IPRENMLMRH SKVTSDGSYI KPPHAKIGYS SMVKVRSRMA MDQGLFLASA
LVIAVRYSAV RRQGYLEDKS REVKVLDYQT QQHRLFPSIA RAYAFIFCGF ETIRLYDQLL
IDVQNGNTSG MADLHALTSG LKSVVTYQTG EGIEQARMAC GGHGYSMASY ISEYYGVAIA
GCTYEGENMV MLLQLARYLV KSIEMIQNGK SRELGPMVAY LAEKESEIDL NLGPNEYLKV
FEYAARNQTW RATEKFQKLR NSGMSNEKAW NQASVELTRA SRLHTRLYIM STFINHVGSI
VDQKVKGVLI DLLNVHVTYE VMDIGIYVQG LLSSNQMDLI RNQLYVSLET IRPNAVSLVD
SFQISDMQLR SVLGRRDGNV YENLFKWAKS SPLNKTDVLP SVTQYLKPMM DKSKL
//
