ACX14_CAEEL
ID ACX14_CAEEL Reviewed; 662 AA.
AC O62139;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Acyl-coenzyme A oxidase acox-1.4 {ECO:0000305};
DE EC=1.3.3.- {ECO:0000305|PubMed:29537254, ECO:0000305|PubMed:29863473};
GN Name=acox-1.4 {ECO:0000312|WormBase:F08A8.4};
GN Synonyms=acox-4 {ECO:0000312|WormBase:F08A8.4};
GN ORFNames=F08A8.4 {ECO:0000312|WormBase:F08A8.4};
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, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF GLU-433 AND
RP 517-TRP--LEU-662.
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).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-433 AND
RP 517-TRP--LEU-662.
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:29537254, PubMed:29863473). Specifically, shortens ascarosides
CC with a 9-carbon side chain (asc-C9) and, in association with acox-1.1,
CC may contribute to the shortening of ascarosides with a 11-carbon side
CC chain (asc-C11) (PubMed:29537254, PubMed:29863473). May contribute to
CC the production of indol-3-carbonyl(IC)-ascarosides in association with
CC acox-1.1 and acox-3 (PubMed:29863473). {ECO:0000269|PubMed:29537254,
CC ECO:0000269|PubMed:29863473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=asc-C9-CoA + O2 = asc-DeltaC9-CoA + H2O2;
CC Xref=Rhea:RHEA:66224, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139617, ChEBI:CHEBI:139706;
CC Evidence={ECO:0000305|PubMed:29537254, ECO:0000305|PubMed:29863473};
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 1.4 folding and/or dimer formation (By similarity).
CC {ECO:0000250|UniProtKB:O62140}.
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:29537254}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O62140}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O62140}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000255|PIRNR:PIRNR000168}.
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DR EMBL; BX284601; CAB16866.1; -; Genomic_DNA.
DR PIR; T20570; T20570.
DR RefSeq; NP_493264.1; NM_060863.4.
DR AlphaFoldDB; O62139; -.
DR SMR; O62139; -.
DR STRING; 6239.F08A8.4.2; -.
DR EPD; O62139; -.
DR PaxDb; O62139; -.
DR PeptideAtlas; O62139; -.
DR EnsemblMetazoa; F08A8.4.1; F08A8.4.1; WBGene00008567.
DR GeneID; 173164; -.
DR KEGG; cel:CELE_F08A8.4; -.
DR UCSC; F08A8.4.1; c. elegans.
DR CTD; 173164; -.
DR WormBase; F08A8.4; CE17636; WBGene00008567; acox-1.4.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000168827; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; O62139; -.
DR OMA; AANPRKW; -.
DR OrthoDB; 226134at2759; -.
DR PhylomeDB; O62139; -.
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; WBGene00008567; Expressed in larva and 1 other tissue.
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..662
FT /note="Acyl-coenzyme A oxidase acox-1.4"
FT /id="PRO_0000452305"
FT MOTIF 660..662
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 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:O62140"
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:O62140"
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:O62140,
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:O62140"
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:O62140"
FT BINDING 341
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 391
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 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: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 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 526..529
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 574
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 MUTAGEN 433
FT /note="E->A: In reb6; accumulation of ascaroside asc-C9 and
FT reduced production of asc-delta-C7 and asc-delta-C9. No
FT defect in indol-3-carbonyl(IC)-ascaroside production.
FT Enhances accumulation of IC-asc-C7 and IC-asc-C9 in a acox-
FT 1.1 (reb2) and acox-3 (tm4033) mutant background."
FT /evidence="ECO:0000269|PubMed:29537254,
FT ECO:0000269|PubMed:29863473"
FT MUTAGEN 517..662
FT /note="Missing: In gk892586; accumulation of ascarosides
FT asc-C7 and asc-C9."
FT /evidence="ECO:0000269|PubMed:29537254"
SQ SEQUENCE 662 AA; 74771 MW; B1EA46F4E920BD68 CRC64;
MHLNTSICEV DNPDLTEERE KGTFDTDKMA AVIYGSEKLA RRRREISEAV SKIPELADTQ
PFPFMDRLEK ITEGSRKLEV LNNNIRDIID YDDNGERLHI YQEVTGMEGH PLALHEVMFI
PALVSQASKE QQEKWLGRAR RREIIGCYAQ TEMGHGTNLR KLETTATYFP DTQEFVLNTP
TTTALKWWPG ALGKSSNYAV VVVDMIIKGK SYGPHPFMVQ LRDEKTHIPL KGIVVGDIGP
KMSFNGGDNG FLGFDKFRVP RTNLLMRHVR VEADGTYVKP PHAKVNHSAM VHVRSHMATG
QGALLAQALI IAVRYSAVRR QGFLENKTQE VKVLDYQTQQ HRLFPSLARA YAFIFTGFET
IHLYSQLLKD VDMGNTSGMA DLHALTSGLK SVVTHQTGEG IEQARMACGG HGYSMASYIS
EIYGIAIGGC TYEGENMVML LQLARYLVKS VELIKSGEAK KLGPMVSYLA AKGGHPDLSS
LNGYVTAFEH MARRQAWKAT EKFLKLMESG ESREIAWNKS TVELTRASRL HTRLFIIEAF
MRRVSRIEDI PVKEVLTDLL HLHVNYELLD VATYALEFMS STQLDYIRDQ LYLYLEKIRP
SAVSLVDSFQ ISDMQLRSVL GRRDGNVYEN LFKWAKSSPL NKSDVLPSVD KYLMPMMEKA
KL
