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Database: UniProt
Entry: A0A0G0IAU8_9BACT
LinkDB: A0A0G0IAU8_9BACT
Original site: A0A0G0IAU8_9BACT 
ID   A0A0G0IAU8_9BACT        Unreviewed;       689 AA.
AC   A0A0G0IAU8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   SubName: Full=Putative acyl-CoA synthetase {ECO:0000313|EMBL:KKQ51632.1};
GN   ORFNames=US70_C0015G0028 {ECO:0000313|EMBL:KKQ51632.1};
OS   Parcubacteria group bacterium GW2011_GWD2_38_11.
OC   Bacteria.
OX   NCBI_TaxID=1618941 {ECO:0000313|EMBL:KKQ51632.1, ECO:0000313|Proteomes:UP000034843};
RN   [1] {ECO:0000313|EMBL:KKQ51632.1, ECO:0000313|Proteomes:UP000034843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKQ51632.1}.
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DR   EMBL; LBTZ01000015; KKQ51632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0IAU8; -.
DR   STRING; 1618941.US70_C0015G0028; -.
DR   Proteomes; UP000034843; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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; 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          9..103
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   689 AA;  75629 MW;  3E0B9538003D8656 CRC64;
     MSKNTLENLF APKSIAIIGA SNKKGKIGTV LVNNVTKLGY KGEVYFVNPS YKLLKLKRCY
     SDLNNIDRHI DVALVAVPAK FVLDVIVASC DKVKNFVVIS AGFSETDAEG MKREKDLAQL
     AKDHNLNILG PNCLGFIAPK LKLNASFAGG MPKAGNIAFV SQSGALAVAL MDRAAQEHIG
     FSQIVSVGNK MQLDESELLE YLAKDKETKV IGMYLEGIKN GQKFIETAKK VSKIKPIVIL
     KAGKTEKAQK AISSHTGALA GSDDIIDVAF EKAGVIRAND LEEFFDLLTL ISFVDAPKNE
     KVAVLTNAGG AGVLTTDAFK GKDIVLADFS SKTKDEMKSV LPQEASVENP VDLLGDAGED
     RYQSILDILN KQKVGVIIPV LTPQQQTPVE KIAEAIIKNR KHSQSAMITV FIGGGRIKKS
     VDDLKKNYIP NFSNPDGAIS ALNKYYKWSL FKKTKEIICK ENINVSRKKQ VEEIIAMAKK
     ENRSALFFSE AFEVMKKYAI NPVSYVEILP GSEISPIMQY PVVIKVDSDK VLHKSDKQAL
     ILNIKDPSAL EAAAKKLRAN FPTERLVVQP MHDKQVEVIL GIKQDSIFGP VIVYGLGGIY
     TEVFKMVNFL IPPMTAQSIK EQILKSKISF LFSGARGQQA YDIEEFASII NGLMDFAVEN
     KNISEFDINP LFIYNDGREA LAVDIKIIL
//
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