ID F4HNK5_PYRSN Unreviewed; 439 AA.
AC F4HNK5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN OrderedLocusNames=PNA2_1235 {ECO:0000313|EMBL:AEC52149.1};
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC52149.1, ECO:0000313|Proteomes:UP000008293};
RN [1] {ECO:0000313|EMBL:AEC52149.1, ECO:0000313|Proteomes:UP000008293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:AEC52149.1,
RC ECO:0000313|Proteomes:UP000008293};
RX PubMed=21602357; DOI=10.1128/JB.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
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; CP002670; AEC52149.1; -; Genomic_DNA.
DR RefSeq; WP_013748702.1; NC_015474.1.
DR AlphaFoldDB; F4HNK5; -.
DR STRING; 342949.PNA2_1235; -.
DR GeneID; 10554715; -.
DR KEGG; pyn:PNA2_1235; -.
DR PATRIC; fig|342949.8.peg.1238; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_3_2; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000008293; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR043938; Ligase_CoA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF19045; Ligase_CoA_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE 4: Predicted;
FT DOMAIN 4..98
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 439 AA; 47822 MW; 8ABAC0FA3DD8E283 CRC64;
MDYFFYPKSV AIFGSFREGS IAREILRNIV EGGFEGKVIP VNPKGGEVEI AGKRFTIKRE
LDEKVDVSII VIPAKLVPDL IRKLKGLTKG AVVISAGFSE VGNVELEDEL VRAAREAGIR
VIGPNCAGIF GVHGKFFGSF EVRVNPGGLA LISQSGAFGG AALAMGNEEG VGFSAFVSYG
NAADLDESDF LRYFAEDENT KVIALYIEGV KDGRKFFEAL KYASKRKPVI ILKAGKSKSG
AKAAASHTGS LAGSYEIYRA VFKQSNVIEV EEMEELFDAA KAFEMYSRAG RRVAVITNSG
GPGVLATDKL ESLGLEIARL SESTVEELRR FLPPQCSVKN PIDLIADADY ERYKRTIEVV
CRDENVDTLL IICVPPIFIP SEEIAKAIID ARCEKPMIVN FMAGSLVEKG VEVLAKYGIK
NFSTPERAAK AIFWLSMRE
//
