ID A0A1G1ILG7_9BACT Unreviewed; 711 AA.
AC A0A1G1ILG7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:OGW69318.1};
GN ORFNames=A2036_01580 {ECO:0000313|EMBL:OGW69318.1};
OS Omnitrophica bacterium GWA2_50_21.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801815 {ECO:0000313|EMBL:OGW69318.1, ECO:0000313|Proteomes:UP000180213};
RN [1] {ECO:0000313|EMBL:OGW69318.1, ECO:0000313|Proteomes:UP000180213}
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:OGW69318.1}.
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DR EMBL; MHFA01000035; OGW69318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ILG7; -.
DR Proteomes; UP000180213; 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; 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}.
FT DOMAIN 500..536
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 711 AA; 77550 MW; 9DF26F6EC97E20BA CRC64;
MTIVRRPLDA IFQPKSVAVI GASRREEAVG HAVFRNMIMG GYKGIVYPVN PKADSILGVR
CYPSVLEIPD EVEMAVLIVP AAAAVQSFRE CIDKGVKGAM VISAGFKEIG GEGVQLEKEL
GRLSKEKGIP LVGPNCLGVI NTDSAVTMNA SFARSMPKPG NIAFISQSGA LCTAVLDYAK
GVNIGFSKFI SMGNKASVTE LELLEYLGQD EQTDVILMYL EDLQRPHDLI RVCRNISGEA
ESPKPILAIK SGRTMQGAKA ASSHTGSLAG SDDVYTAVFT QAGILRVNSV NELFDYAKAF
SARRLPSGNR TAIVTNAGGP GIMATDACVR YGSEMALLSD KTQEELKKFL PPTASVINPV
DVIGDAQHER YEAALKVVLR DKHVDGTIVI LTPQAMTDIE EIAEVIGKVA QKSKKPVLAC
FMGIVDVSKG VTVLEKWKVP HYRFPESAAR SMAAMARYAA WIGRPRTEIR QFTVDTEKAR
SVFWNAWKEK RKALTDFETM SLLTAYGFPT LPMELCKTPE QAAESAERIG YPVVLKINSP
DILHKIDVGG VKLNLNSANQ VLKEAGDMLS RIRKQIPKAN ILGVTVQRMA EKGREVIFGI
KRDPQFGPIL MFGMGGTYVE VMKDVIFRLA PVRQLGAYNM IHAIKAYKIL EGVRGDKPAD
FARLEECLER LSQLAVECPE IEELDINPFL IYEKGRGGVV LDARVLLTGA E
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