ID   A0A1I6D7H1_9FIRM        Unreviewed;       711 AA.
AC   A0A1I6D7H1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SFR01399.1};
GN   ORFNames=SAMN05660706_106135 {ECO:0000313|EMBL:SFR01399.1};
OS   Desulfoscipio geothermicus DSM 3669.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=1121426 {ECO:0000313|EMBL:SFR01399.1, ECO:0000313|Proteomes:UP000199584};
RN   [1] {ECO:0000313|Proteomes:UP000199584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3669 {ECO:0000313|Proteomes:UP000199584};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOYM01000006; SFR01399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6D7H1; -.
DR   STRING; 39060.SAMN05660706_106135; -.
DR   Proteomes; UP000199584; 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   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199584};
KW   Transferase {ECO:0000313|EMBL:SFR01399.1}.
FT   DOMAIN          504..540
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   711 AA;  76007 MW;  982374E1A967D20F CRC64;
     MATYSTNKRV KKMADLNGFF NPRSVAIVGA SKTPGKIGNA IIKNIVNSGF SGKIYPVNPK
     AEEIEGLPCY PNISAVQDPV DLAVVTIPAD RVLDAARECA GQGVKHLVVI TAGFKEVGKE
     GLDLEKKLVA ICREHGINML GPNCVGMMNT HARLNASFSG AYPKQGDIAF ISQSGAMLVA
     ILDWSIKTGL GFSKVISLGN KAQLNEADFI EAVAQDPGTR VILCYIEDVA DGEHFLQVAA
     RATREKPVII LKSGTSQAGA MAASSHTGAL AGSDLAYETA FRQCGVIRAH SMPELFDLAI
     AFSAQPIPPN ANVAVVTNAG GPGIVATDRV ETSGLNMARF SKETIDILRK ELPAESNIYN
     PVDVLGDAGA DRYHLALDKV LADPSVGSAV VLVCPTAVTD PLPTARAIVD LHHRYPDKPV
     LAAYMGGPML SAGAELLSAE GIPCFTFPEP AIEAISGMNR YAELSKNKFA AEEMEIQVDD
     ETVRNVLSAV RQDGRLVLLG SESYQVAAAY GIPAAPVELA TSPEEAVELA EKIGYPVVMK
     VASPKIMHKT DVGGVKINLA DADAVRRGYI EINENIQRYL PDVVIHGIEV QKMMPKGVEL
     IVGMSRDVQF GPLIAFGLGG IYVNLLKDVS FRLARGLTRR EIETMLTETK AYTLLRGYRG
     EKPADIGTLV EIIARVARLV TDFNEITEMD INPVFAYPRG ASALDIKITI S
//