ID B6YWM6_THEON Unreviewed; 472 AA.
AC B6YWM6;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
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_1001 {ECO:0000313|EMBL:ACJ16489.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ16489.1, ECO:0000313|Proteomes:UP000002727};
RN [1] {ECO:0000313|EMBL:ACJ16489.1, ECO:0000313|Proteomes:UP000002727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ16489.1,
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; ACJ16489.1; -; Genomic_DNA.
DR RefSeq; WP_012571961.1; NC_011529.1.
DR AlphaFoldDB; B6YWM6; -.
DR STRING; 523850.TON_1001; -.
DR GeneID; 7017305; -.
DR KEGG; ton:TON_1001; -.
DR PATRIC; fig|523850.10.peg.1009; -.
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 12..111
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 472 AA; 51568 MW; A7DFC163C8895172 CRC64;
MEAKIVEEMR PFFDPRAVAI IGATNKKGKV GNVIFENFKM NKERGIFKGN IYPVNPKLDE
IDGYKVYKSV EELPDDTDLA VISIPAPFVP DTMRQIAKKG IKAVIIITGG FGELGEEGKK
LEREILEIAR ENGIRIIGPN CVGVYVPDTG VDTVFLPENK MDRPKSGPIA FVSQSGAFAA
AMLDWAAMAD IGIGKMVSYG NKLDVDDADL MDYFIHDDSI NVVTFYIEGV KDGRKFMEAA
RRITKVKPVI ALKSGRTEYG AKAASSHTGS LAGADTIYDA VFKQTGVIRA EDFEHMFDLA
KAFAALKDKL PKGNRIGIIT DGGGAGVMAS DAVAKFGLKM AELSEETLKF LKENFPPHAV
AGNPTDVVGD TDAERYRIAI EGFVNDPNVD AILVIVLFQV PLLEEEKIID ILAEYQKKSD
KPIVAVAMGG KKTDYYARIL EEKGVPVYPT PERGVRALAG LVKYAEYLRR GD
//
