ACX13_CAEEL
ID ACX13_CAEEL Reviewed; 660 AA.
AC O62138;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Acyl-coenzyme A oxidase acox-1.3 {ECO:0000305};
DE EC=1.3.3.- {ECO:0000269|PubMed:25775534};
GN Name=acox-1.3 {ECO:0000312|WormBase:F08A8.3};
GN Synonyms=acox-3 {ECO:0000303|PubMed:25775534,
GN ECO:0000312|WormBase:F08A8.3};
GN ORFNames=F08A8.3 {ECO:0000312|WormBase:F08A8.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20610393; DOI=10.1074/jbc.m110.122663;
RA Joo H.J., Kim K.Y., Yim Y.H., Jin Y.X., Kim H., Kim M.Y., Paik Y.K.;
RT "Contribution of the peroxisomal acox gene to the dynamic balance of
RT daumone production in Caenorhabditis elegans.";
RL J. Biol. Chem. 285:29319-29325(2010).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP INTERACTION WITH ACOX-1.1, AND INDUCTION.
RX PubMed=25775534; DOI=10.1073/pnas.1423951112;
RA Zhang X., Feng L., Chinta S., Singh P., Wang Y., Nunnery J.K.,
RA Butcher R.A.;
RT "Acyl-CoA oxidase complexes control the chemical message produced by
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3955-3960(2015).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=29537254; DOI=10.1021/acschembio.7b01021;
RA Zhang X., Wang Y., Perez D.H., Jones Lipinski R.A., Butcher R.A.;
RT "Acyl-CoA Oxidases Fine-Tune the Production of Ascaroside Pheromones with
RT Specific Side Chain Lengths.";
RL ACS Chem. Biol. 13:1048-1056(2018).
CC -!- FUNCTION: Involved in the first step of peroxisomal beta-oxidation by
CC catalyzing the desaturation of fatty acid-derived side chains of
CC ascaroside pheromones, which regulates development and behavior
CC (PubMed:20610393, PubMed:25775534, PubMed:29537254). Specifically,
CC shortens ascarosides with a 7-carbon side chain (asc-C7)
CC (PubMed:25775534, PubMed:29537254). Does not catalyze the desaturation
CC of fatty acids or hydroxylated fatty acids (PubMed:25775534,
CC PubMed:29537254). Involved in the biosynthesis of asc-C6-MK (daumone 2)
CC and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1); daumones are
CC pheromones produced during unfavourable growth conditions which promote
CC entry into the dauer stage (PubMed:20610393).
CC {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:25775534,
CC ECO:0000269|PubMed:29537254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=asc-C7-CoA + O2 = asc-DeltaC7-CoA + H2O2;
CC Xref=Rhea:RHEA:66216, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139646, ChEBI:CHEBI:139712;
CC Evidence={ECO:0000269|PubMed:25775534};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O62137};
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 1.3 folding and/or dimer formation (By similarity).
CC {ECO:0000250|UniProtKB:O62140}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex
CC with acox-1.1) {ECO:0000269|PubMed:25775534};
CC Note=kcat is 144 sec(-1) with asc-C7-CoA (at 30 degrees Celsius, pH
CC 7.4 and in complex with acox-1.1). {ECO:0000269|PubMed:25775534};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:25775534}.
CC -!- SUBUNIT: Forms a heterodimer with acox-1.1; the interaction may be
CC important for the stability of acox-1.3. {ECO:0000269|PubMed:25775534}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O62140}.
CC -!- INDUCTION: Induced by high temperatures (25 degrees Celsius)
CC (PubMed:20610393). Induced by starvation (PubMed:25775534).
CC {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:25775534}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown abolishes production of
CC dauer pheromone daumone 2, severely reduces production of daumone 3 and
CC increases production of daumone 1. {ECO:0000269|PubMed:20610393}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000255|PIRNR:PIRNR000168}.
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DR EMBL; BX284601; CAB16865.1; -; Genomic_DNA.
DR PIR; T20569; T20569.
DR RefSeq; NP_493263.1; NM_060862.1.
DR AlphaFoldDB; O62138; -.
DR SMR; O62138; -.
DR STRING; 6239.F08A8.3; -.
DR PaxDb; O62138; -.
DR PeptideAtlas; O62138; -.
DR EnsemblMetazoa; F08A8.3.1; F08A8.3.1; WBGene00008566.
DR GeneID; 184167; -.
DR KEGG; cel:CELE_F08A8.3; -.
DR UCSC; F08A8.3; c. elegans.
DR CTD; 184167; -.
DR WormBase; F08A8.3; CE17635; WBGene00008566; acox-1.3.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000168827; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; O62138; -.
DR OMA; TKWWIGA; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; O62138; -.
DR BRENDA; 1.3.3.6; 1045.
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 Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008566; Expressed in larva and 2 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:1904070; P:ascaroside biosynthetic process; IMP:UniProtKB.
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:UniProtKB.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
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 1: Evidence at protein level;
KW ATP-binding; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Nucleotide-binding; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..660
FT /note="Acyl-coenzyme A oxidase acox-1.3"
FT /id="PRO_0000452304"
FT MOTIF 658..660
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000168-1"
FT BINDING 146..149
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:O62140"
FT BINDING 154..155
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:O62140"
FT BINDING 188
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:O62140,
FT ECO:0000255|PIRSR:PIRSR000168-2"
FT BINDING 282..285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O62137"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O62137"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:O62140"
FT BINDING 337..340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:O62140"
FT BINDING 339
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 389
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 393
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 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:O62140"
FT BINDING 430..431
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O62137"
FT BINDING 433
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:O62140"
FT BINDING 572
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"
SQ SEQUENCE 660 AA; 74781 MW; 4E255D878FDB4234 CRC64;
MSSICKGDNS DLTEERKNAT FDTDKMAAVI YGREEIASRR RQLTESISRI HELAESKPLV
FMTREEKIAE SCRKLEVLSR HWNQTPFNRD NEEDALHIYR EVLGMEGHPL ALHDTMFIPT
LVAQASQEQQ EKWLGRARRK EIIGCYAQTE MGHGTNLRKL ETTATYSPDT QEFILNTPTI
TALKWWPGAL GKSSNNAIVV ANLLIKDQNY GPHPFMVQLR DEKTHIPLKG IVVGDIGPKM
AFNGADNGYL GFNNHRIPRT NLLMRHTKVE ANGTYIKPSH AKIGYSSMVK VRSRMAMDQG
LFLASALVIA VRYSAVRRQG FLEDKTQKVK VLDYQTQQHR LFPSLARAYA FIFTGFETIH
LYSQLLKDVD MGNTSGMADL HALTSGLKSV VTHQTGEGIE QARMACGEHG YSMASYISEI
YGVAIGGCTY EGENMVMLLQ LARYLVKSVE LIKSGEEKKL GPMVSYLAAK GGHPDLSSLN
GYVTAFEHMA RRQAWKATEK FLKLMETGES REVAWNKSAV ELTRASRLHT RLFIIEAFMR
RVSRIEDIPV KEVLTDLLHL HVNYELLDVA TYALEFMSST QLDYIRDQLY LYLEKIRPSA
VSLVDSFQIS DMQLRSVLGR RDGNVYENLF KWAKSSPLNK SDVLPSVDKY LKPMMEKAKL
