ID   Q5JG99_THEKO            Unreviewed;       232 AA.
AC   Q5JG99;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE            EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN   OrderedLocusNames=TK0465 {ECO:0000313|EMBL:BAD84654.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD84654.1, ECO:0000313|Proteomes:UP000000536};
RN   [1] {ECO:0000313|EMBL:BAD84654.1, ECO:0000313|Proteomes:UP000000536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC   {ECO:0000313|Proteomes:UP000000536};
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC         Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456216; EC=6.2.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001619};
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DR   EMBL; AP006878; BAD84654.1; -; Genomic_DNA.
DR   RefSeq; WP_011249420.1; NC_006624.1.
DR   AlphaFoldDB; Q5JG99; -.
DR   STRING; 69014.TK0465; -.
DR   EnsemblBacteria; BAD84654; BAD84654; TK0465.
DR   GeneID; 78446976; -.
DR   KEGG; tko:TK0465; -.
DR   PATRIC; fig|69014.16.peg.457; -.
DR   eggNOG; arCOG01338; Archaea.
DR   HOGENOM; CLU_063044_1_1_2; -.
DR   InParanoid; Q5JG99; -.
DR   OrthoDB; 18103at2157; -.
DR   PhylomeDB; Q5JG99; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000536}.
FT   DOMAIN          27..63
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   232 AA;  25835 MW;  15992381CBF87541 CRC64;
     MDRIAKAREI IEKAKAENRP LVEPEAKEIL RLYGVPVPDF KVATNEEEAV KFAREIGYPV
     VMKIVSPQII HKSDAGGVKV NIKNDEEARQ AFRTIMENAR NYKPDADLWG VIIYRMLPLG
     KEVIVGMIRD PQFGPAIMFG LGGIFVEILK DVSFRVAPIS KDEALEMIKE IKAYPILAGA
     RGEKPVDIEA LADIIVKVGE LALELPEIRE LDINPIFAYE DGAVAVDARM LL
//