ID B6YXJ0_THEON Unreviewed; 459 AA.
AC B6YXJ0;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN OrderedLocusNames=TON_1313 {ECO:0000313|EMBL:ACJ16803.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ16803.1, ECO:0000313|Proteomes:UP000002727};
RN [1] {ECO:0000313|EMBL:ACJ16803.1, ECO:0000313|Proteomes:UP000002727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ16803.1,
RC ECO:0000313|Proteomes:UP000002727};
RX PubMed=18790866; DOI=10.1128/JB.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.S., Kwon K.K., Kim H.T., Park C.J., Lee H.W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.J., Lee J.H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16803.1; -; Genomic_DNA.
DR RefSeq; WP_012572275.1; NC_011529.1.
DR AlphaFoldDB; B6YXJ0; -.
DR STRING; 523850.TON_1313; -.
DR GeneID; 7018341; -.
DR KEGG; ton:TON_1313; -.
DR PATRIC; fig|523850.10.peg.1321; -.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_3_2; -.
DR OrthoDB; 18103at2157; -.
DR Proteomes; UP000002727; 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..100
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 459 AA; 49667 MW; 4E1B5D997EC7545C CRC64;
MTFDYFFKPK AIAVIGASND PLKLGYEVFK NLKDYKDGKV YPVNVKDEVV QGVKAYKNVK
DIPDEVELAV VVVPKRFVKQ TIIDCGEKGV KGIILITAGF GEVGEDGKRE ERELVEIAHR
YGMRIVGPNC VGIMNTHNDM NATFVANAKK GDIAFISQSG ALGAGIIYKT IKEGIGFSKF
VSIGNMADVD FAEFMEYLAN DPESKAIALY IEGIKDGRKF MEVAKRVTKK KPVIVLKAGK
SESGARAASS HTGSLAGSYK IYEAAFKQSG IIVADTIDDM LSMARAFTQP LPKGKRVAIM
TNAGGPGVLT ADEIDKRGLK LANLEEKTMG GLRSFLPPMA AVKNPVDMIA SARGEDYYRT
AKLLLEDPNV DMLIAICVVP TFAGMTPTEH AEGVVRAVKE VNNGKPVLGL FMAGYISEPA
KEVLEKAGIP SYERPEDVAS AAYALVEFAK DVGILKEEK
//