ID   A0A0G0FJL2_9BACT        Unreviewed;       689 AA.
AC   A0A0G0FJL2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   SubName: Full=Putative acyl-CoA synthetase {ECO:0000313|EMBL:KKQ13835.1};
GN   ORFNames=US27_C0008G0018 {ECO:0000313|EMBL:KKQ13835.1};
OS   Candidatus Moranbacteria bacterium GW2011_GWF1_36_78.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1618718 {ECO:0000313|EMBL:KKQ13835.1, ECO:0000313|Proteomes:UP000034485};
RN   [1] {ECO:0000313|EMBL:KKQ13835.1, ECO:0000313|Proteomes:UP000034485}
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:KKQ13835.1}.
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DR   EMBL; LBSI01000008; KKQ13835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0FJL2; -.
DR   PATRIC; fig|1618718.3.peg.607; -.
DR   Proteomes; UP000034485; 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          6..104
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   689 AA;  75272 MW;  07422154A22F190A CRC64;
     MSLDKLFNPK SIAIVGASSE EGKIGNVIAK NILELGYGGE VYLVNPKYAE IFGKKCYKSL
     GEIPTSSAGM IDLAILAIPA KFVNQEILNN SKNIKNYVVI SAGFSEIGEE GKKQEEELKK
     ITKENGLNIL GPNCLGFIIP SLKLNASFAG GMPEAGNIAF VSQSGALAVA IMDAAKKEGT
     KFSSIVSVGN KMQISETEML EFLGQDENTK VIGMYLEGIK EGGKFIEIAG KIAKIKPIVI
     LKAGKNEKTQ KAISSHTGAL AGNDEIVSAV FEKSGIIRAN NLEEFFALLN FISFSNTVPN
     QKVAVITNAG GAGVLVSDAF SGKKIKLADL ENETKNKLRE FLPAESSVEN PIDLLGDARA
     DRYKKALKII SSAPEIGSVI CLLTPQEQTP VAEIAKEIIK FKDKTDKNIV TVFLGGEKVE
     KAITKLKQNE VCNFSFPDLA VTAIDSYSQW NEFGVVKTKT QTQLINEKRR AKVLEIIAKA
     KSENRQALYF GESAEVMAMY EINTVESFEI ENYHGRNLGY PVVLKVDSDK VLHKTDKNGV
     ILNIENEMNL SRAVSQIKTN FPESHLIIQP MAKKGAELII GIKKDEIFGP VIVYGLGGIY
     AEFLKTVDYL VPPLSLAQME KTLLSGKIKF LFQGARGQKK YNVEEMVKIL MGISSFALEI
     PEIREFDINP LIVYNNSQEA VAVDVKIMI
//