ACX11_CAEEL
ID ACX11_CAEEL Reviewed; 674 AA.
AC O62140; Q2L6T9; Q7JK62;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Acyl-coenzyme A oxidase acox-1.1 {ECO:0000305};
DE EC=1.3.3.- {ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473};
DE EC=1.3.3.6 {ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473};
GN Name=acox-1.1 {ECO:0000312|WormBase:F08A8.1a};
GN Synonyms=acox-1 {ECO:0000312|WormBase:F08A8.1a};
GN ORFNames=F08A8.1 {ECO:0000312|WormBase:F08A8.1a};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP 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 SUBUNIT, AND INTERACTION WITH ACOX-1.2 AND ACOX-1.3.
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, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-396 AND GLU-434.
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 [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLU-434.
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).
RN [6] {ECO:0007744|PDB:5K3G, ECO:0007744|PDB:5K3H, ECO:0007744|PDB:5K3I}
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF APO FORM AND MUTANT ALA-434 IN
RP COMPLEX WITH ATP AND FAD, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, PATHWAY, SUBUNIT, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP VAL-118; TRP-189; TYR-245; GLY-301; GLN-340; LYS-391; HIS-396; GLU-434;
RP ASN-437; ARG-533 AND ARG-536.
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).
CC -!- FUNCTION: Involved in the first step of peroxisomal beta-oxidation by
CC catalyzing the desaturation of fatty acid-derived side chains
CC (PubMed:25775534, PubMed:29537254, PubMed:27551084). Specifically,
CC catalyzes the desaturation of fatty acids heptanoyl-CoA (C7), nonanoyl-
CC CoA (C9), dodecanoyl-CoA (C12) and to a lesser extent pentanoyl-CoA
CC (C5) and hexadecanoyl-CoA (C16), and hydroxylated fatty acid
CC hydroxynonanoyl-CoA (PubMed:25775534, PubMed:29537254,
CC PubMed:27551084). Also, catalyzes the desaturation fatty acid-derived
CC side chains of ascaroside pheromones, which regulates development and
CC behavior (PubMed:20610393, PubMed:25775534, PubMed:29537254,
CC PubMed:29863473, PubMed:27551084). Specifically, shortens ascaroside
CC with 5-carbon omega side chain (asc-omega-C5), 7-carbon side chain
CC (asc-C7), 9-carbon side chain (asc-C9), 11-carbon side chain (asc-C11),
CC 13-carbon side chain (asc-C13), 15-carbon side chain (asc-C15) and to a
CC lesser extent ascarosides with 7-omega-carbon side chain (asc-omega-C7)
CC (PubMed:25775534, PubMed:29537254, PubMed:27551084). Also shortens
CC indol-3-carbonyl(IC)-ascarosides with 7-carbon side chain (IC-asc-C7)
CC and to a lesser extent (IC)-ascarosides with 9-carbon side chain (IC-
CC asc-C9) (PubMed:29863473). May associate and regulate the folding
CC and/or the catalytic activity of other acyl-coenzyme A oxidases
CC including acox-1.2, acox-1.3, acox-1.4 and acox-3 modulating the type
CC of ascarosides produced (PubMed:25775534, PubMed:29537254,
CC PubMed:29863473). In association with acox-1.3, catalyzes the
CC desaturation of asc-C7-CoA but not of fatty acids or hydroxylated fatty
CC acids (PubMed:25775534). Involved in the biosynthesis of asc-C6-MK
CC (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1);
CC daumones are pheromones produced during unfavourable growth conditions
CC which promote entry into the dauer stage (PubMed:20610393).
CC {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:25775534,
CC ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254,
CC ECO:0000269|PubMed:29863473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nonanoyl-CoA + O2 = (2E)-nonenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38987, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:76291, ChEBI:CHEBI:76292;
CC Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:29537254,
CC ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40171, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57330, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254,
CC ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084,
CC ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heptanoyl-CoA + O2 = (2E)-heptenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:66204, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:78811, ChEBI:CHEBI:166980;
CC Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8R)-8-hydroxynonanoyl-CoA + O2 = (2E,8R)-8-hydroxynonenoyl-
CC CoA + H2O2; Xref=Rhea:RHEA:66208, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:166978, ChEBI:CHEBI:166979;
CC Evidence={ECO:0000269|PubMed:25775534};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + pentanoyl-CoA = (2E)-pentenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:66200, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57389, ChEBI:CHEBI:86160;
CC Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000269|PubMed:27551084};
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-omegaC5-CoA + O2 = asc-omegaDeltaC5-CoA + H2O2;
CC Xref=Rhea:RHEA:66212, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:140060, ChEBI:CHEBI:166969;
CC Evidence={ECO:0000269|PubMed:25775534};
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, ECO:0000269|PubMed:27551084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=asc-omegaC7-CoA + O2 = asc-omegaDeltaC7-CoA + H2O2;
CC Xref=Rhea:RHEA:66220, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139994, ChEBI:CHEBI:140057;
CC Evidence={ECO:0000269|PubMed:27551084};
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:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084,
CC 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: Activated by ATP (PubMed:27551084). ATP binding
CC leads to a conformational change that promotes FAD cofactor binding and
CC enzyme activity (PubMed:27551084). ATP binding likely occurs during
CC acox-1.1 folding and/or dimer formation (PubMed:27551084).
CC {ECO:0000269|PubMed:27551084}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42.7 uM for asc-C9-CoA (at 30 degrees Celsius and pH 7.4)
CC {ECO:0000269|PubMed:25775534};
CC KM=60 uM for asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex
CC with acox-1.3) {ECO:0000269|PubMed:25775534};
CC KM=152 uM for asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in
CC complex with acox-1.2) {ECO:0000269|PubMed:25775534};
CC Note=kcat is 252 sec(-1) with asc-C9-CoA (at 30 degrees Celsius and
CC pH 7.4) (PubMed:25775534). kcat is 144 sec(-1) with asc-C7-CoA (at 30
CC degrees Celsius, pH 7.4 and in complex with acox-1.3)
CC (PubMed:25775534). kcat is 478 sec(-1) with asc-omega-C5-CoA (at 30
CC degrees Celsius, pH 7.4 and in complex with acox-1.2)
CC (PubMed:25775534). {ECO:0000269|PubMed:25775534};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084,
CC ECO:0000269|PubMed:29537254}.
CC -!- SUBUNIT: Homodimer (Probable). Forms a heterodimer with acox-1.2
CC (PubMed:25775534). Forms a heterodimer with acox-1.3; the interaction
CC may be important for the stability of acox-1.3 (PubMed:25775534).
CC {ECO:0000269|PubMed:25775534, ECO:0000305|PubMed:27551084}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:20610393,
CC ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F08A8.1a};
CC IsoId=O62140-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F08A8.1b};
CC IsoId=O62140-2; Sequence=VSP_060949;
CC Name=c {ECO:0000312|WormBase:F08A8.1c};
CC IsoId=O62140-3; Sequence=VSP_060950;
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis and intestine.
CC {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:29863473}.
CC -!- INDUCTION: Induced by high temperatures (25 degrees Celsius).
CC {ECO:0000269|PubMed:20610393}.
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; CAB16867.1; -; Genomic_DNA.
DR EMBL; BX284601; CAE54894.1; -; Genomic_DNA.
DR EMBL; BX284601; CAJ58493.1; -; Genomic_DNA.
DR PIR; T20571; T20571.
DR RefSeq; NP_001021089.1; NM_001025918.4. [O62140-1]
DR RefSeq; NP_001021090.1; NM_001025919.3. [O62140-2]
DR RefSeq; NP_001040649.1; NM_001047184.2. [O62140-3]
DR PDB; 5K3G; X-ray; 2.86 A; A/B/C/D=1-674.
DR PDB; 5K3H; X-ray; 2.48 A; A/B/C/D/E/F/G/H=1-674.
DR PDB; 5K3I; X-ray; 2.68 A; A/B/C/D/E/F/G/H=1-674.
DR PDBsum; 5K3G; -.
DR PDBsum; 5K3H; -.
DR PDBsum; 5K3I; -.
DR AlphaFoldDB; O62140; -.
DR SMR; O62140; -.
DR IntAct; O62140; 1.
DR MINT; O62140; -.
DR STRING; 6239.F08A8.1a.2; -.
DR EPD; O62140; -.
DR PaxDb; O62140; -.
DR PeptideAtlas; O62140; -.
DR EnsemblMetazoa; F08A8.1a.1; F08A8.1a.1; WBGene00008564. [O62140-1]
DR EnsemblMetazoa; F08A8.1a.2; F08A8.1a.2; WBGene00008564. [O62140-1]
DR EnsemblMetazoa; F08A8.1b.1; F08A8.1b.1; WBGene00008564. [O62140-2]
DR EnsemblMetazoa; F08A8.1b.2; F08A8.1b.2; WBGene00008564. [O62140-2]
DR EnsemblMetazoa; F08A8.1c.1; F08A8.1c.1; WBGene00008564. [O62140-3]
DR GeneID; 173162; -.
DR KEGG; cel:CELE_F08A8.1; -.
DR UCSC; F08A8.1b.4; c. elegans.
DR CTD; 173162; -.
DR WormBase; F08A8.1a; CE17633; WBGene00008564; acox-1.1.
DR WormBase; F08A8.1b; CE36125; WBGene00008564; acox-1.1.
DR WormBase; F08A8.1c; CE39570; WBGene00008564; acox-1.1.
DR eggNOG; KOG0136; Eukaryota.
DR GeneTree; ENSGT00940000168827; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; O62140; -.
DR OMA; WMITQQT; -.
DR OrthoDB; 416859at2759; -.
DR PhylomeDB; O62140; -.
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; WBGene00008564; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; O62140; baseline and differential.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:WormBase.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IDA:UniProtKB.
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 3D-structure; Alternative splicing; ATP-binding; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Nucleotide-binding;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..674
FT /note="Acyl-coenzyme A oxidase acox-1.1"
FT /id="PRO_0000452302"
FT MOTIF 672..674
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 434
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000168-1"
FT BINDING 149..152
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:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 157..158
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:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 191
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:0000255|PIRSR:PIRSR000168-2,
FT ECO:0000269|PubMed:27551084, ECO:0007744|PDB:5K3I"
FT BINDING 285..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O62137"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O62137"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 340..343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 342
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 392
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:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 396
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:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 411
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 433..434
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O62137"
FT BINDING 436
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 533..536
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:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT BINDING 581
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:0000269|PubMed:27551084,
FT ECO:0007744|PDB:5K3I"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060949"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060950"
FT MUTAGEN 118
FT /note="V->A: Shows catalytic activity toward asc-omega-C5-
FT CoA without affecting activity toward asc-C9-CoA, asc-
FT omega-C7-CoA or fatty acyl-CoA; when associated with F-245
FT and E-301."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 189
FT /note="W->A: Loss of ATP and FAD binding."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 245
FT /note="Y->F: Shows catalytic activity toward asc-omega-C5-
FT CoA without affecting activity toward asc-C9-CoA, asc-
FT omega-C7-CoA or fatty acyl-CoA; when associated with A-118
FT and E-301."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 301
FT /note="G->E: Reduced catalytic activity toward ascaroside
FT asc-C9-CoA, but not toward fatty acyl-CoA substrates. Has a
FT slight activity toward asc-omega-C5-CoA. Shows catalytic
FT activity toward asc-omega-C5-CoA without affecting activity
FT toward asc-C9-CoA, asc-omega-C7-CoA or fatty acyl-CoA; when
FT associated with A-118 and F-245."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 340
FT /note="Q->A: Loss of ATP and FAD binding."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 391
FT /note="K->A: Loss of ATP binding and severe reduction in
FT FAD binding."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 396
FT /note="H->G: Loss of ATP and FAD binding. Severe loss of
FT catalytic activity toward ascaroside-CoA and fatty acyl-CoA
FT substrates. Defects in the processing of ascarosides with
FT 13-, 11-, 9-, and 7-carbon side chains. No defect in
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:27551084,
FT ECO:0000269|PubMed:29537254"
FT MUTAGEN 434
FT /note="E->A: In reb2; severe reduction in catalytic
FT activity toward fatty-acid CoA and ascaroside-CoA.
FT Increases ATP and FAD binding. No defect in the production
FT of various ascarosides apart from a slight accumulation of
FT asc-C11. Accumulation of indol-3-carbonyl (IC)-asc-C7.
FT Enhances accumulation of IC-asc-C7 and IC-asc-C9 in a acox-
FT 1.4 (reb6) and acox-3 (tm4033) mutant background."
FT /evidence="ECO:0000269|PubMed:27551084,
FT ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473"
FT MUTAGEN 437
FT /note="N->A: Loss of ATP binding and severe reduction in
FT FAD binding."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 533
FT /note="R->E: Loss of ATP binding."
FT /evidence="ECO:0000269|PubMed:27551084"
FT MUTAGEN 536
FT /note="R->E: Loss of ATP binding."
FT /evidence="ECO:0000269|PubMed:27551084"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5K3H"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5K3H"
FT TURN 191..196
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:5K3H"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 298..319
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 338..365
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5K3I"
FT HELIX 383..402
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:5K3H"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:5K3I"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:5K3I"
FT HELIX 438..456
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 465..471
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 488..515
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 528..553
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 557..577
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 579..584
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:5K3I"
FT HELIX 590..616
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 636..645
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:5K3H"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:5K3H"
FT HELIX 662..668
FT /evidence="ECO:0007829|PDB:5K3H"
SQ SEQUENCE 674 AA; 76074 MW; FED79A75F936FECD CRC64;
MVHLNKTIQE GDNPDLTAER LTATFDTHAM AAQIYGGEMR ARRRREITAK LAEIPELHDS
MPLPYMTREE KIMESARKLT VLTQRMSEII DPTDAGELYH LNNEVLGIEG NPMALHGVMF
IPALNAQASD EQQAKWLIRA LRREIIGTYA QTEMGHGTNL QNLETTATYD IGTQEFVLHT
PKITALKWWP GNLGKSSNYA VVVAHMYIKG KNFGPHTFMV PLRDEKTHKP LPGITIGDIG
PKMAYNIVDN GFLGFNNYRI PRTNLLMRHT KVEADGTYIK PPHAKINYSA MVHVRSYMLT
GQAIMLSYAL NIATRYSAVR RQGQIDKNEP EVKVLEYQTQ QHRLFPFIAR AYAFQFAGAE
TVKLYERVLK EMKSGNVSLM ADLHALTSGL KSVVTHQTGE GIEQARMACG GHGYSMASYI
SEIYGVAIGG CTYEGENMVM LLQLARYLVK SAALVKSGKA SQLGPLVAYL GARSEPTSLI
DRVPNGGITE YIKTFQHIAK RQTLKAANKF FGLMENGEKR EIAWNKSSVE LNRASRLHTR
LFIVEAFARR VNEIGDITIK EALSDLLHLH VNYELLDVAT YALEDGFMSS TQLDYVRDQL
YFYLQKIRPN AVSLLDSWEF SDRELRSVLG RRDGHVYENL FKWAKESPLN KTDVLPSVDT
YLKPMMEKAR QSKL
