ID   G4E1S8_9GAMM            Unreviewed;       893 AA.
AC   G4E1S8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=CoA-binding domain protein {ECO:0000313|EMBL:EGZ50572.1};
GN   ORFNames=ThisiDRAFT_0257 {ECO:0000313|EMBL:EGZ50572.1};
OS   Thiorhodospira sibirica ATCC 700588.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiorhodospira.
OX   NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ50572.1};
RN   [1] {ECO:0000313|EMBL:EGZ50572.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ50572.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EGZ50572.1}.
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; AGFD01000003; EGZ50572.1; -; Genomic_DNA.
DR   RefSeq; WP_006786258.1; NZ_MU255056.1.
DR   AlphaFoldDB; G4E1S8; -.
DR   STRING; 765914.ThisiDRAFT_0257; -.
DR   PATRIC; fig|765914.3.peg.267; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG0456; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   OrthoDB; 9807426at2; -.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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; PS51186; GNAT; 1.
PE   4: Predicted;
FT   DOMAIN          737..893
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   893 AA;  97400 MW;  536C26E25C57515A CRC64;
     MGPHYLNRFF SAKSIAVIGA SERADAVGSL VFANLISAGY QGDLYPINLK RDTIQGYKAY
     PDVEAIGRPV DLVVIATPAR TVPPLIRQCG AFGIRSAVVL SAGFGEAGSV GRRLQEAMID
     AAREYDVRII GPNCLGIMRP SQGLNATFSK NSALKGDLAL VSQSGAICTA ILDWAETQQI
     GFSAVASMGD TADVDFGDVL DYLALDRETH SILVYVEGVR NARRFMSGLR AAARIKPVIV
     IKSGRKEEGS RAAMSHTGAI VGADDVFDAS LERAGAVRAL TISQLFSAAR ILSSRYRVES
     NRLAIISNAG GPGVMATDRA VEVDIELAQL TPESIKALNE VLPDHWSHGN PIDILGDADA
     PRYEKAISIC LSDPNIDGAL VMLTPQAMTQ PTEVAQAVID AAKKTEKPVM ASWMGGEQVR
     AGRELFTKHH LPHFSTPEAS VEAFAYLAAH QRNQKMLLQV PGPLSDRIKT DVSGARMIIE
     GALSEGRKTL STMESKAVLS AFRIPVTQTV QARSANEALV AAGTVGYPVA MKIDSPDITH
     KSDVGGVKLN IVSAEAVRSA YQAMVEEARR VAPQARIQGV TVERMYKSTY GRELMIGVIR
     DPAFGPVVSF GSGGTSVEVM KDRAVALPPL NEFIIQNMIE RTKVARMLKQ FRNMPPVDTE
     ALEMVLLRVS EMACELPEIQ ELDINPLIVD ERGLAAVDAR ISVDYPAPMS DRYAHMAIHP
     YPNHWVTQWQ LSDGTTLVIR PIRPEDAKIE QEFVRKLSAE SRYFRFMQAV HELTPQMLVR
     FTQIDYDREM ALIAVHERPD GSELQVAVAR YTANPDQRSC EFALAVADEW KGKGIGSHLM
     HYLMDVAKKK GIDVMEGEIL SQNSNMLALV KRLKFSTHVS PEDDSIIMAS KRL
//