ID I3RGC8_9EURY Unreviewed; 252 AA.
AC I3RGC8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=Py04_1719 {ECO:0000313|EMBL:AFK23288.1};
OS Pyrococcus sp. ST04.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=1183377 {ECO:0000313|EMBL:AFK23288.1, ECO:0000313|Proteomes:UP000006467};
RN [1] {ECO:0000313|EMBL:AFK23288.1, ECO:0000313|Proteomes:UP000006467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST04 {ECO:0000313|EMBL:AFK23288.1,
RC ECO:0000313|Proteomes:UP000006467};
RX PubMed=22843576; DOI=10.1128/JB.00824-12;
RA Jung J.H., Lee J.H., Holden J.F., Seo D.H., Shin H., Kim H.Y., Kim W.,
RA Ryu S., Park C.S.;
RT "Complete Genome Sequence of the Hyperthermophilic Archaeon Pyrococcus sp.
RT Strain ST04, Isolated from a Deep-Sea Hydrothermal Sulfide Chimney on the
RT Juan de Fuca Ridge.";
RL J. Bacteriol. 194:4434-4435(2012).
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; CP003534; AFK23288.1; -; Genomic_DNA.
DR RefSeq; WP_014734808.1; NC_017946.1.
DR AlphaFoldDB; I3RGC8; -.
DR STRING; 1183377.Py04_1719; -.
DR GeneID; 13022997; -.
DR KEGG; pys:Py04_1719; -.
DR eggNOG; arCOG01338; Archaea.
DR HOGENOM; CLU_063044_1_1_2; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000006467; 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}.
FT DOMAIN 26..62
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 252 AA; 28420 MW; 1BEC7CE68AFE9086 CRC64;
MREEAVKVIE EVLKQGRTAM VEYEAKQVLK AYGLPVPEEK LAKTLDEALV YAKEIGYPVA
MKLMSPQILH KSDARVVMLN IKDEEELKKK WEEIHENAKK YNPNAEILGV LIAPMLKPGR
EVIIGVTEDP QFGHAIMFGL GGIFVEILKD VTFRLVPITE KDARKMITEI KAYPILAGAR
GEEPADIDAI VDMLLKVSKL VDDLRDYIKE MDLNPVFVYN KGEGAVIVDA RIILKSGEEK
KPEGEYREER CA
//
