ID A0A1F5A0B9_9BACT Unreviewed; 692 AA.
AC A0A1F5A0B9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=CoA-binding domain-containing protein {ECO:0000259|SMART:SM00881};
GN ORFNames=A2Y86_00930 {ECO:0000313|EMBL:OGD12039.1};
OS Candidatus Aminicenantes bacterium RBG_13_62_12.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797269 {ECO:0000313|EMBL:OGD12039.1, ECO:0000313|Proteomes:UP000178836};
RN [1] {ECO:0000313|EMBL:OGD12039.1, ECO:0000313|Proteomes:UP000178836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD12039.1}.
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DR EMBL; MEXX01000016; OGD12039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5A0B9; -.
DR STRING; 1797269.A2Y86_00930; -.
DR Proteomes; UP000178836; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP 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; 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.
PE 4: Predicted;
FT DOMAIN 5..100
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
SQ SEQUENCE 692 AA; 75095 MW; 588BCAD9A4BEDE72 CRC64;
MLDALFKPRS VAIIGASSNP LSIGHIVLKN LLDHDFKGPI YPINPKAVSI KSLRSYASIT
DVPDEVDLVN ISIKNTLVPA VLEECGKKGV KFAIVHTAGF KETGEEGRRL EERIVAVAHD
HGLRIFGPNS QGIQNSDPAV SVYANFTFVP MSPGNISIVA QSGGVGETLK LQLYKIGKGI
RMYASFGNEA DVSLNEIVEY YGQDEKTRAI MVHVETLRDP AGFLEVASRV SPRKPILALK
TGRTSEGAVA VASHTGSLME QDTLTDVIFK KSGVLRFHSQ EEMINAAIAF SSQPVPKGDR
AVIVTNTGGP AIIAVDECVS AGLKLAKLSD TTKERLKKLV FQEAIVSNPV DVVATAGPDQ
YGGTVAALLE DPNIDSLLLV FVTAPFVDCE GIARRLGELG RTATKPIICQ VITIEKWAEV
IRLIRDSGIP VYDYAETAAR VLGAMTQHGK FLQREAPSSI RFKVEKPTAD KIFERSKEKK
AFLRQDEAFS LLESYGIRTV KTFRVETEGD LEKAAAKIAF PVVLKVDSEE IIHKTEAGGV
ALNLKNKTEL LAAFATMAKT FAPQKPGYVL QAQAEAGLEM ILGLKGNQGL APTMMFGLGG
VFVETLRDVQ FRLTPLSKQD VLEMIRSIKS YGLLEGARGE SPRDIEVLAE MMMRLSQLGT
DVPWIDELDL NPVLVYENGK GAIVVDVRIR AA
//
