ID F8C4V1_THEGP Unreviewed; 699 AA.
AC F8C4V1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Acetyl coenzyme A synthetase (ADP forming), alpha domain protein {ECO:0000313|EMBL:AEH22735.1};
GN OrderedLocusNames=TOPB45_0633 {ECO:0000313|EMBL:AEH22735.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH22735.1, ECO:0000313|Proteomes:UP000006583};
RN [1] {ECO:0000313|EMBL:AEH22735.1, ECO:0000313|Proteomes:UP000006583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH22735.1,
RC ECO:0000313|Proteomes:UP000006583};
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
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DR EMBL; CP002829; AEH22735.1; -; Genomic_DNA.
DR RefSeq; WP_013909435.1; NC_015682.1.
DR AlphaFoldDB; F8C4V1; -.
DR STRING; 795359.TOPB45_0633; -.
DR KEGG; top:TOPB45_0633; -.
DR PATRIC; fig|795359.3.peg.643; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_0; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000006583; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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 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; IPR014089; AcCoA-synth-alpha.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 NCBIfam; TIGR02717; AcCoA-syn-alpha; 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 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006583}.
FT DOMAIN 491..527
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 699 AA; 76397 MW; B7EBF92A5366531F CRC64;
MLDFIFKPNS IAVIGASEDE KKIGHVVFRN LVKQGFEGKV YPVNPKREEI LGIKCYPSVK
DLPEKIDLAI IVIPAKGVPS VIKDCASAGV KGLIVITAGF REIGGEGIKL EQEIVELVKK
YGIRMVGPNC LGVINTINKM NATFASELPP CGRVSFFSQS GALGVALIDW AIENNFGFGK
FVSLGNKADL NETDFLEYFG EDPETDIILG YIEDIKDGKR FLEVAKKVSK IKPVIIIKAG
TTEAGAKAAS SHTGAFAGFD RAFSEAFKKA GIIRVNSIKE LFETAEIFKL NKIPKGDRLL
VITNAGGPGI IAADTADKLG IKLDPMSEES IEAIIDKLPP TASLYNPIDI IGDATSERYK
VVLEQAIKDR YVDGICVILT PQAVTDVENV ATEIVRISQN TEKPVFACFI GGKKVSSAIK
ILKSQQIPCY SDPSVAISSY KKLIDFSIIK NKKEPEIPKI EISLENKEKV RLILEILENA
GVSSVGEENA TEILSLYGFN FPKKALAKTP EEAVEIAEKI GYPVVLKVSS PNILHKTDVG
GVKLNLKNAE EVYNAFVDIT INVKRFMPNA YIKGVMVYEM ITGGKEVILG VSYDTTFGHM
LMFGLGGIYV EVLKDVSFRI APLTKEEAYE MVEEIKGAKI LEGVRGEPPY DKENIVDKIL
RLSQLVTDFP IIKEIDINPY VVKHQGGVAL DARMIIGKL
//