ID   W0I529_9EURY            Unreviewed;       463 AA.
AC   W0I529;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-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=TES1_1846 {ECO:0000313|EMBL:AHF81221.1};
OS   Thermococcus paralvinellae.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF81221.1, ECO:0000313|Proteomes:UP000019027};
RN   [1] {ECO:0000313|EMBL:AHF81221.1, ECO:0000313|Proteomes:UP000019027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES1 {ECO:0000313|EMBL:AHF81221.1,
RC   ECO:0000313|Proteomes:UP000019027};
RX   PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA   Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT   "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT   of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL   Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
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; CP006965; AHF81221.1; -; Genomic_DNA.
DR   RefSeq; WP_042682303.1; NZ_CP006965.1.
DR   AlphaFoldDB; W0I529; -.
DR   STRING; 582419.TES1_1846; -.
DR   GeneID; 24907510; -.
DR   KEGG; ths:TES1_1846; -.
DR   HOGENOM; CLU_007415_2_3_2; -.
DR   OrthoDB; 18103at2157; -.
DR   Proteomes; UP000019027; 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          6..104
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   463 AA;  50063 MW;  23D236FD4DABB692 CRC64;
     MNLDFLFYPK SVAVIGASHV SGKIGNAIMR SITRQFNGKI YAVNVKGGEI EVNGKKFKVY
     KSILDVPDEV DVAVIAVPAK FVPDVIDECG QKGVKGAIVI SAGFKEAGRA DLEEELVKRA
     RKWGIHVVGP NCLGVTNLEN GFDCNFNPPE RQARPKFGGI AFMSQSGAFG AAILDWAARH
     EVGMSKFISL GNMADLDESD FMSYLKDDPK TKVITAYLEG VKDGRKFFNI AKETTKVKPV
     IVLKAGRTEA GAKAAASHTG SLAGSYAIYE AAFEQTGVLS AKSMRQLFNY AKALAMQKPA
     KGDRVAIVTN GGGAGVMMSD GLLEKGLKLA QLSDETNEKF AKAIEEGKLP HHMSYKNPID
     VIGDAPSKRY ELAMRYALED PNVDVLVVIA LFQSPALDEG IVDVMEKVQE YGKPIVFVAP
     GGEYPEKMAR RIEEKGVPVF ETVEDGVDAV YALVKYGKYL SGV
//