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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//