ID   ACX15_CAEEL             Reviewed;         659 AA.
AC   P34355;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Probable acyl-coenzyme A oxidase acox-1.5 {ECO:0000305};
DE            Short=AOX 1.5 {ECO:0000305};
DE            Short=Acyl-CoA oxidase 1.5 {ECO:0000312|WormBase:C48B4.1};
DE            EC=1.3.3.- {ECO:0000250|UniProtKB:O62140};
GN   Name=acox-1.5 {ECO:0000312|WormBase:C48B4.1};
GN   Synonyms=acox-5 {ECO:0000312|WormBase:C48B4.1};
GN   ORFNames=C48B4.1 {ECO:0000312|WormBase:C48B4.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Involved in the first step of peroxisomal beta-oxidation by
CC       catalyzing the desaturation of fatty acid-derived side chains.
CC       {ECO:0000250|UniProtKB:O62140}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O62140};
CC   -!- ACTIVITY REGULATION: Activated by ATP (By similarity). ATP binding
CC       leads to a conformational change that promotes FAD cofactor binding and
CC       enzyme activity (By similarity). ATP binding likely occurs during acox-
CC       1.5 folding and/or dimer formation (By similarity).
CC       {ECO:0000250|UniProtKB:O62140}.
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:O62140}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O62140}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O62140}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; Z29117; CAA82376.1; -; Genomic_DNA.
DR   PIR; S40722; S40722.
DR   RefSeq; NP_499119.1; NM_066718.6.
DR   AlphaFoldDB; P34355; -.
DR   SMR; P34355; -.
DR   BioGRID; 41548; 3.
DR   FunCoup; P34355; 1479.
DR   STRING; 6239.C48B4.1.1; -.
DR   PaxDb; 6239-C48B4.1.1; -.
DR   PeptideAtlas; P34355; -.
DR   EnsemblMetazoa; C48B4.1.1; C48B4.1.1; WBGene00008167.
DR   GeneID; 176353; -.
DR   KEGG; cel:CELE_C48B4.1; -.
DR   UCSC; C48B4.1.1; c. elegans.
DR   AGR; WB:WBGene00008167; -.
DR   CTD; 176353; -.
DR   WormBase; C48B4.1; CE00491; WBGene00008167; acox-1.5.
DR   eggNOG; KOG0136; Eukaryota.
DR   HOGENOM; CLU_014629_3_1_1; -.
DR   InParanoid; P34355; -.
DR   OMA; ICTRFSA; -.
DR   OrthoDB; 538336at2759; -.
DR   PhylomeDB; P34355; -.
DR   Reactome; R-CEL-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-CEL-389887; Beta-oxidation of pristanoyl-CoA.
DR   UniPathway; UPA00661; -.
DR   PRO; PR:P34355; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00008167; Expressed in larva and 4 other cell types or tissues.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
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:0042811; P:pheromone biosynthetic process; IMP:CACAO.
DR   CDD; cd01150; AXO; 1.
DR   FunFam; 1.10.540.10:FF:000006; Acyl-coenzyme A oxidase; 1.
DR   FunFam; 1.20.140.10:FF:000005; Acyl-coenzyme A oxidase; 1.
DR   FunFam; 1.20.140.10:FF:000013; Acyl-coenzyme A oxidase; 1.
DR   FunFam; 2.40.110.10:FF:000003; Acyl-coenzyme A oxidase; 1.
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; IPR034171; ACO.
DR   InterPro; IPR055060; ACOX_C_alpha1.
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:SF304; ACYL-COENZYME A OXIDASE ACOX-1.5-RELATED; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF22924; ACOX_C_alpha1; 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; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Nucleotide-binding; Oxidoreductase; Peroxisome; Reference proteome.
FT   CHAIN           1..659
FT                   /note="Probable acyl-coenzyme A oxidase acox-1.5"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000204688"
FT   MOTIF           657..659
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        433
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P07872"
FT   BINDING         148..151
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         156..157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O62137,
FT                   ECO:0000255|PIRSR:PIRSR000168-2"
FT   BINDING         284..287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         319
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         339..342
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O62140"
FT   BINDING         403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         410
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         432..433
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         435
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
FT   BINDING         524..527
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:O62137"
SQ   SEQUENCE   659 AA;  74714 MW;  5F0D6E92F8CAA5F8 CRC64;
     MPLNKLIQDG DNQDLTDERF KATFDTDALA AVFHGGEDAL KRIRELRDEV TKRWHLFDAL
     PGAHRTRAER MEDVSRKLKN LMESVGEFAD FTNNLDMLVI IRDVMGIEGF PLALHNLMFV
     PTIQNQADDE QTEWWLMDAL QGKIIGTYAQ TELGHGTNLG AIETTATYDK LTEEFIIHTP
     TTTATKWWPG GLGTSCTHVV LVANLIIDTK NYGLHPFFVP IRDRNSYSVM SGVRVGDIGT
     KMGVNCVDNG FLAFDNYRIP RRNMLMKHSK VSKEGLYTAP SHPKVGYTTM LYMRSEMIYH
     QAYYLAMAMA ISIRYSAVRR QGEIKPGTQE VQILDYQTQQ YRIFPGLARC FAFNTAAATV
     RQMTENCIKQ LSHGNSDVLA DLHALSCGLK AVVTHQASQS IDQARQACGG HGYSDASYLP
     TLYTCSVGAC TYEGENMVML LQLSKYLMKA AAKAEKGEEM APLVAYLVKP DITETNDKFA
     KMLSHFEHIA RHRVMHAYRQ MIEEEKQGIE RDYAFANHSV DWTKAARAHT KLFIARGFVK
     SVQEVSDEAV HDVLTTLAEL YLSYELIEMS ADLTANGYLS ESDVQQIRHQ IYDSMRKTRR
     NAVSIVDSFD ICDRELRSVL GRRDGHVYEN LYKWAQMSPL NERNLPHVEK YLKPMTSKL
//