ID Q5JIA9_THEKO Unreviewed; 243 AA.
AC Q5JIA9;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN OrderedLocusNames=TK0943 {ECO:0000313|EMBL:BAD85132.1};
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:BAD85132.1, ECO:0000313|Proteomes:UP000000536};
RN [1] {ECO:0000313|EMBL:BAD85132.1, 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; BAD85132.1; -; Genomic_DNA.
DR RefSeq; WP_011249894.1; NC_006624.1.
DR AlphaFoldDB; Q5JIA9; -.
DR SMR; Q5JIA9; -.
DR STRING; 69014.TK0943; -.
DR EnsemblBacteria; BAD85132; BAD85132; TK0943.
DR GeneID; 78447456; -.
DR KEGG; tko:TK0943; -.
DR PATRIC; fig|69014.16.peg.921; -.
DR eggNOG; arCOG01338; Archaea.
DR HOGENOM; CLU_063044_1_1_2; -.
DR InParanoid; Q5JIA9; -.
DR OrthoDB; 18103at2157; -.
DR PhylomeDB; Q5JIA9; -.
DR BRENDA; 6.2.1.13; 5246.
DR BRENDA; 6.2.1.B10; 5246.
DR BRENDA; 6.2.1.B11; 5246.
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 28..64
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 243 AA; 27148 MW; E32C6E133F2AE29D CRC64;
MSAKEEALKV IESVLKSGRT ALVEYEAKQV LKAYSLPVPN EKLAKTLDEA LEYAEEIGYP
VAMKLMSPQI LHKSDAKVVI LNIKSPEELK QKWEEIHENA RKYRPDAEIL GVLIAPMLRP
GREIIIGVTE DPQFGHAIMF GLGGIFVEVL KDVTFRIIPI TEKDARKMIA EIKGYPILAG
ARGEEPADID AIVDMLLKVS QLVDELRDYI KEMDLNPVFV YEKGKGAVVV DARIIAKAPE
KKE
//
