ACS7_CAEEL
ID ACS7_CAEEL Reviewed; 540 AA.
AC Q17577;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Acyl-CoA synthetase 7 {ECO:0000303|PubMed:29863473};
DE EC=6.2.1.- {ECO:0000269|PubMed:29863473, ECO:0000305|PubMed:32702987};
GN Name=acs-7 {ECO:0000312|WormBase:C01G6.7};
GN ORFNames=C01G6.7 {ECO:0000312|WormBase:C01G6.7};
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=28371259; DOI=10.1002/anie.201700103;
RA Panda O., Akagi A.E., Artyukhin A.B., Judkins J.C., Le H.H., Mahanti P.,
RA Cohen S.M., Sternberg P.W., Schroeder F.C.;
RT "Biosynthesis of Modular Ascarosides in C. elegans.";
RL Angew. Chem. Int. Ed. 56:4729-4733(2017).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF 186-SER-SER-187 AND GLU-339.
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 [4] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32702987; DOI=10.1021/jacs.0c04223;
RA Faghih N., Bhar S., Zhou Y., Dar A.R., Mai K., Bailey L.S., Basso K.B.,
RA Butcher R.A.;
RT "A Large Family of Enzymes Responsible for the Modular Architecture of
RT Nematode Pheromones.";
RL J. Am. Chem. Soc. 142:13645-13650(2020).
CC -!- FUNCTION: Plays a role in ascaroside pheromones biosynthesis, which
CC regulates development and behavior (PubMed:29863473, PubMed:28371259,
CC PubMed:32702987). Specifically, activates the side chain of medium-
CC chain indol-3-carbonyl (IC)-ascarosides for shortening through beta-
CC oxidation (PubMed:29863473, PubMed:32702987). Converts IC-asc-C7 and
CC IC-asc-C9 into IC-asc-C7-CoA and IC-asc-C9-CoA, respectively
CC (PubMed:29863473, PubMed:32702987). May play a role in fatty-acid
CC metabolism by activating and converting nonanoate (C9) into nonanoyl-
CC CoA (C9-CoA) (PubMed:29863473). {ECO:0000269|PubMed:28371259,
CC ECO:0000269|PubMed:29863473, ECO:0000269|PubMed:32702987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + nonanoate = AMP + diphosphate + nonanoyl-CoA;
CC Xref=Rhea:RHEA:54952, ChEBI:CHEBI:30616, ChEBI:CHEBI:32361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:76291,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + IC-asc-C7 = AMP + diphosphate + IC-asc-C7-CoA;
CC Xref=Rhea:RHEA:66252, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:166976, ChEBI:CHEBI:166981,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29863473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + IC-asc-C9 = AMP + diphosphate + IC-asc-C9-CoA;
CC Xref=Rhea:RHEA:66240, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:166973, ChEBI:CHEBI:166984,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:29863473,
CC ECO:0000305|PubMed:32702987};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.5 uM for IC-asc-C9 (at pH 7.4 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:29863473};
CC Note=kcat is 0.53 sec(-1) with IC-asc-C9 (at pH 7.4 and 22 degrees
CC Celsius). {ECO:0000269|PubMed:29863473};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:29863473}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine.
CC {ECO:0000269|PubMed:28371259, ECO:0000269|PubMed:29863473}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284602; CAA84640.1; -; Genomic_DNA.
DR PIR; T18841; T18841.
DR RefSeq; NP_495979.1; NM_063578.4.
DR AlphaFoldDB; Q17577; -.
DR SMR; Q17577; -.
DR STRING; 6239.C01G6.7; -.
DR EPD; Q17577; -.
DR PaxDb; Q17577; -.
DR PeptideAtlas; Q17577; -.
DR EnsemblMetazoa; C01G6.7.1; C01G6.7.1; WBGene00007228.
DR GeneID; 174472; -.
DR KEGG; cel:CELE_C01G6.7; -.
DR UCSC; C01G6.7; c. elegans.
DR CTD; 174472; -.
DR WormBase; C01G6.7; CE00869; WBGene00007228; acs-7.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q17577; -.
DR OMA; ILIEYYA; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q17577; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007228; Expressed in larva and 3 other tissues.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IDA:UniProtKB.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:1904070; P:ascaroside biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Peroxisome;
KW Reference proteome.
FT CHAIN 1..540
FT /note="Acyl-CoA synthetase 7"
FT /id="PRO_0000452470"
FT MOTIF 538..540
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 186..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT MUTAGEN 186..187
FT /note="SS->AA: Loss of catalytic activity; when associated
FT with A-339."
FT /evidence="ECO:0000269|PubMed:29863473"
FT MUTAGEN 339
FT /note="E->A: Severe loss of catalytic activity. Loss of
FT catalytic activity; when associated with 186-A-A-187."
FT /evidence="ECO:0000269|PubMed:29863473"
SQ SEQUENCE 540 AA; 60637 MW; F3F49C1D64920688 CRC64;
MIFHGEQLEN HDKPVHEVLL ERFKVHQEKD PDNVAFVTAE NEDDSLGFQQ LGKKVLQISE
WFVENGYKKG DVFLLASYNN WRCFAAALGA WRAGLIVSAA ASQFTSFEMN YQIEDSQSQV
ILVDKHTLPV VQEACKNLKF VKQIISISAN PPSPVIKFDV LTSRLVRNLK MPLIDPKNDI
VFLPYSSGTT GKPKGVMISH LNFSMMLESS LRFFDANAKA IGLPPDFVLP YDLHFLPMYH
AMGMFRTLLT SYRGTTQIMF TKFDMELMLK NIEKYSIMVL SLVPAIAVRM LNSPLLQKYD
VSSLVSVTVG SAPFPESASK KLKQLLPNVN IVQGYGMTEL TFATHLQSPG SPDGSVGRLV
PGTSMKVKKE DGTLCGPHEI GELWIKGPQM MKGYWKKEQQ TNELLDEHGF MRTGDIVYFD
KNGETFICDR IKELIKVNAK QVAPAELESV ILEHDDVADV CVFGVDDASS GERPVACVVS
KRGRDMETSK AIMKHINQKL ARYKHIKEIE FVSEIMRTGT GKLLRRAMKK AFLDAKKAKL
