ID A0A0T6AGM6_9BACT Unreviewed; 714 AA.
AC A0A0T6AGM6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=CoA-binding domain-containing protein {ECO:0000313|EMBL:KRT74141.1};
GN ORFNames=XU13_C0009G0006 {ECO:0000313|EMBL:KRT74141.1};
OS Candidatus Rokubacteria bacterium CSP1-6.
OC Bacteria; Candidatus Rokubacteria.
OX NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT74141.1, ECO:0000313|Proteomes:UP000051916};
RN [1] {ECO:0000313|EMBL:KRT74141.1, ECO:0000313|Proteomes:UP000051916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT74141.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT74141.1}.
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DR EMBL; LDXP01000009; KRT74141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AGM6; -.
DR STRING; 1640509.XU13_C0009G0006; -.
DR PATRIC; fig|1640509.3.peg.662; -.
DR Proteomes; UP000051916; Unassembled WGS sequence.
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; 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 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}.
FT DOMAIN 498..534
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 714 AA; 75397 MW; 6EF62C0CDD15EDC5 CRC64;
MSRAALDRLF RPRSIALLGA SEDFVKISGR PLKFLLDKGY GGKIFPVNPK YTTLAGLPCY
PNVAAIPEPV DLAIVALPAA AVVDAVTQCA ARGIPAAVVF SSGFGEVGED GRRLELQLAE
AARRGGLRLC GPNTLGFMNT FDRVMATFSQ AGEGEASEGP VAFVTQSGAF GTAIFALARQ
RGLPFGYFVN SGNEADLDFA DLLDYVVADP RVRVAAGYIE GLKDGRKLLA VSERALELGK
PLVVAKVGRS SAGARAALSH TGSLAGSDRV YSGVFRQKGI VRAAHDEELL DLVSAFLHCP
LPEGRGVGIV TQSGGAGVLM ADRAEEIGLV VPELAEETKE RLRKVIPAFG SAKNPVDITA
QFIADPGLLR SSLEIVLQDP HVDAAIFYLG LMERFADQVV ANLREVHAGA KKPLLVAWAG
APEAGLRALG QSGICVLPSA ARAVNAVRGL VEYAEARSRW KQSRGAESRP GGGREQIQSL
VRACRSEGRR VLTTGESFGL LSRYGVRVAR SRLSRTPAEA AQAAEEIGYP VALKIESPAI
RHKTEAKALR LDVAGRQEVL RAFQEVVTEA RRHAPEADIH GVLVQEMVRD GTEVVVGVHH
DPQFGPVVMV GLGGIFVEVL EDVSFRAAPL SREDAEQMVA ELRGARVLEG VRGRPPADVP
SLIEALMAVS RLAADAAGEI AELDVNPLLV LPGGRGAVAV DALTVLAEPG TGSP
//
