ACX3_CAEEL
ID ACX3_CAEEL Reviewed; 667 AA.
AC Q20992;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Acyl-coenzyme A oxidase acox-3 {ECO:0000305};
DE EC=1.3.3.- {ECO:0000269|PubMed:29863473};
GN Name=acox-3 {ECO:0000312|WormBase:F58F9.7};
GN Synonyms=acox-6 {ECO:0000312|WormBase:F58F9.7};
GN ORFNames=F58F9.7 {ECO:0000312|WormBase:F58F9.7};
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 COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=27551084; DOI=10.1073/pnas.1608262113;
RA Zhang X., Li K., Jones R.A., Bruner S.D., Butcher R.A.;
RT "Structural characterization of acyl-CoA oxidases reveals a direct link
RT between pheromone biosynthesis and metabolic state in Caenorhabditis
RT elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10055-10060(2016).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=29863473; DOI=10.7554/elife.33286;
RA Zhou Y., Wang Y., Zhang X., Bhar S., Jones Lipinski R.A., Han J., Feng L.,
RA Butcher R.A.;
RT "Biosynthetic tailoring of existing ascaroside pheromones alters their
RT biological function in C. elegans.";
RL Elife 7:0-0(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:29863473). Specifically, shortens indol-3-carbonyl(IC)-
CC ascarosides with 7-carbon (IC-asc-C7) or 9-carbon (IC-asc-C9) side
CC chains and contributes to the shortening of ascarosides with 13-carbon
CC (asc-C13) and 15-carbon (asc-C15) side chains (PubMed:29863473).
CC {ECO:0000269|PubMed:29863473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IC-asc-C7-CoA + O2 = H2O2 + IC-asc-DeltaC7-CoA;
CC Xref=Rhea:RHEA:66232, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:166976, ChEBI:CHEBI:166977;
CC Evidence={ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IC-asc-C9-CoA + O2 = H2O2 + IC-asc-DeltaC9-CoA;
CC Xref=Rhea:RHEA:66236, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:166973, ChEBI:CHEBI:166974;
CC Evidence={ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=asc-C13-CoA + O2 = asc-DeltaC13-CoA + H2O2;
CC Xref=Rhea:RHEA:66228, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139652, ChEBI:CHEBI:139655;
CC Evidence={ECO:0000269|PubMed:29863473};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27551084};
CC -!- ACTIVITY REGULATION: In contrast to other acyl-coenzyme A oxidases
CC which bind to and are activated by ATP, does not bind ATP.
CC {ECO:0000269|PubMed:27551084}.
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:29863473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O62140}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:29863473}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine.
CC {ECO:0000269|PubMed:29863473}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000255|PIRNR:PIRNR000168}.
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DR EMBL; BX284604; CCD67635.1; -; Genomic_DNA.
DR PIR; T28847; T28847.
DR RefSeq; NP_500943.1; NM_068542.4.
DR AlphaFoldDB; Q20992; -.
DR SMR; Q20992; -.
DR STRING; 6239.F58F9.7.1; -.
DR EPD; Q20992; -.
DR PaxDb; Q20992; -.
DR PeptideAtlas; Q20992; -.
DR EnsemblMetazoa; F58F9.7.1; F58F9.7.1; WBGene00019060.
DR GeneID; 177386; -.
DR KEGG; cel:CELE_F58F9.7; -.
DR UCSC; F58F9.7.1; c. elegans.
DR CTD; 177386; -.
DR WormBase; F58F9.7; CE07304; WBGene00019060; acox-3.
DR eggNOG; KOG0135; Eukaryota.
DR GeneTree; ENSGT00940000159423; -.
DR HOGENOM; CLU_014629_4_2_1; -.
DR InParanoid; Q20992; -.
DR OMA; YVTRAPI; -.
DR OrthoDB; 226134at2759; -.
DR PhylomeDB; Q20992; -.
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 IV.
DR Bgee; WBGene00019060; Expressed in larva and 3 other tissues.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IBA:GO_Central.
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:0016402; F:pristanoyl-CoA oxidase activity; 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 CDD; cd01150; AXO; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR034171; ACO.
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; 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 PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..667
FT /note="Acyl-coenzyme A oxidase acox-3"
FT /id="PRO_0000452301"
FT MOTIF 665..667
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 433
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000168-1"
FT BINDING 138..141
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 146..147
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 178
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 313
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 334..337
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 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 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"
SQ SEQUENCE 667 AA; 74887 MW; 7B0C4DA3A9F446F4 CRC64;
MSAPLIDKYR KMATFDWKKL KAAVEGEEHV RLKSEVVAKM KSEPVFHRDY RVLSREEQRE
VVHQRWKKIV EWGLFKDPYS DLENFHALTE TLEAYDQGTS ARLFLHGNVF GAAVKSMGTD
RHKDLIQKTE NNEIVGAFCL TEVGHGSNTA EIQTTATFDN GELVFNTPSV SAIKCWAGNL
AHSATHVVVY AQLHVEGKNE GFHGFVIQVR CPRTFQTLPG ITIGDMGSKP GCWQGVENGW
MEFKNHRAPL SALLNKGCDI TPDGKYVTSF KSASEKQSVS LGTLSVGRLG IIAKGMMACT
FASTIAIRYS VARRQFGPVK GAENEIPVLE YPLQQYRLFP YLSAAICIRI FQKKFVGHFT
EYMMRVIMGE KSDELSEFSK EVHALSSGAK PVATWLGVES LGEARKACGG HGYLQMSRLN
TLRDDNDPSQ TFEGENFMIL QQTSNILLGK AQSIGSIETP MSTMSFLNQK PSKFSSWSSN
PVNDVLSAYR YLTYHLLQTT SAEAYRLKAS GKNSFEVRNE IQIHRAVNLS VAYTEHTMIH
WVQQFLKEIE DQSVKPVLQK VLNLFSLFLL ERHLATLYIT GYASGGKFGE DLREKLRLAV
AELKPEAIAL VDSIAPDDFI LHSALGASDG KAYEHIMEEF RKYTNEQPRW VCDLAQFLQK
RSQGSKL
