ID A0A075LUG9_9EURY Unreviewed; 232 AA.
AC A0A075LUG9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=PAP_06970 {ECO:0000313|EMBL:AIF69786.1};
OS Palaeococcus pacificus DY20341.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Palaeococcus.
OX NCBI_TaxID=1343739 {ECO:0000313|EMBL:AIF69786.1, ECO:0000313|Proteomes:UP000027981};
RN [1] {ECO:0000313|Proteomes:UP000027981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY20341 {ECO:0000313|Proteomes:UP000027981};
RA Zeng X., Shao Z.;
RT "Complete Genome Sequence of Hyperthermophilic Palaeococcus pacificus
RT DY20341T, Isolated from a Deep-Sea Hydrothermal Sediments.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIF69786.1, ECO:0000313|Proteomes:UP000027981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY20341 {ECO:0000313|EMBL:AIF69786.1,
RC ECO:0000313|Proteomes:UP000027981};
RX PubMed=26383653;
RA Zeng X., Jebbar M., Shao Z.;
RT "Complete Genome Sequence of Hyperthermophilic Piezophilic Archaeon
RT Palaeococcus pacificus DY20341T, Isolated from Deep-Sea Hydrothermal
RT Sediments.";
RL Genome Announc. 3:e01080-e01015(2015).
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; CP006019; AIF69786.1; -; Genomic_DNA.
DR RefSeq; WP_048165306.1; NZ_CP006019.1.
DR AlphaFoldDB; A0A075LUG9; -.
DR STRING; 1343739.PAP_06970; -.
DR GeneID; 24842507; -.
DR KEGG; ppac:PAP_06970; -.
DR eggNOG; arCOG01338; Archaea.
DR HOGENOM; CLU_063044_1_1_2; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000027981; 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 27..63
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 232 AA; 25725 MW; 4372D1D1A1FB9F8F CRC64;
MERIEKARQI IEKAKAEGRP LVEPEAKEIL KLYGVPVPDF KVATNEEEAV QFAREIGYPV
VMKIVSPQII HKSDAGGVKV NIKSDEEARE AFKKIMENAK NYKPDADLWG VIVYKMLPLG
KEVIVGMIRD PQFGPAIMFG LGGIFVEILK DVSFRVAPIT KDEALDMIKE IKAYPILAGA
RGEKPVNIEA LADIIAKVGE LALELPEVKE LDINPIFAYE DEAVAVDARM LL
//
