ACX15_CAEEL
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 03-AUG-2022, entry version 152.
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_066718.3.
DR AlphaFoldDB; P34355; -.
DR SMR; P34355; -.
DR BioGRID; 41548; 2.
DR STRING; 6239.C48B4.1; -.
DR EPD; P34355; -.
DR PaxDb; P34355; -.
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 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; PMMRGKL; -.
DR OrthoDB; 416859at2759; -.
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 Reactome; R-CEL-9033241; Peroxisomal protein import.
DR UniPathway; UPA00661; -.
DR PRO; PR:P34355; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00008167; Expressed in larva and 4 other tissues.
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:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0042811; P:pheromone biosynthetic process; IMP:CACAO.
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; IPR009075; AcylCo_DH/oxidase_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; PF00441; Acyl-CoA_dh_1; 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 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
