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Database: UniProt
Entry: A0A1I6CP56_9FIRM
LinkDB: A0A1I6CP56_9FIRM
Original site: A0A1I6CP56_9FIRM 
ID   A0A1I6CP56_9FIRM        Unreviewed;       704 AA.
AC   A0A1I6CP56;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SFQ94973.1};
GN   ORFNames=SAMN05660706_10199 {ECO:0000313|EMBL:SFQ94973.1};
OS   Desulfoscipio geothermicus DSM 3669.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=1121426 {ECO:0000313|EMBL:SFQ94973.1, 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; FOYM01000001; SFQ94973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6CP56; -.
DR   STRING; 39060.SAMN05660706_10199; -.
DR   Proteomes; UP000199584; Unassembled WGS sequence.
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; IPR011761; ATP-grasp.
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.
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:SFQ94973.1}.
FT   DOMAIN          498..549
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   704 AA;  75470 MW;  2026DA03B6A71CBE CRC64;
     MTQKHDLEPF VNPQSVALIG VSSRTGPGTF NVLEQMLSRG YRGRVYPVNP RGGTILGVPA
     YRSVADIDAP VDLAVISTPR TAVPGLVRQC AEKGIKSVVI ITQGFSDADD EAGARMHREI
     VETVRSTGIR VVGPNTLGVI NTFNNFSTSF LKFDVTNSPV GVICQSGIFL AAAQDFTGGI
     GIGIDIGNTS DIGFTECMEY LAGDDRIKVI NLHMEGLQDG RRFLQAARRV TPQKPVLVLK
     TGSSEEGARA AGSHSGSLAG EDAVFSAAFA QCGIIRVEDS ARLAELNRTF ATYRHMAGKR
     IGVMTISGGA GIMAVDACSK YGLKTAGLAP KTREVLESVF PDWMHAGNPA DIWPAGMAKG
     YGKIAALALE TILADDGVDA VLGITPAYVH PDEDPLNIVG PVNEIAARYP HKPTALWVFG
     PHKERYAERF RETGAVVVYS SPDDAMYCLA RLYRYHNEIK GKTYPAFRPP QDIDRGKAGI
     VLAAGRRAGL PALNEQALDI MEAYGIPVVR RGLAENREEA LRLAEKLGYP VVMKIASPDI
     THKSDASGVQ LNINSPEALA LAYGEMMDNV RRRKPEARIE GVLLQNQASG GTEVILGGRR
     DPQFGPVLVY GLGGIFTELM RDVAFRVAPV TPVEALDMIK QTKSYKILSG ARGRAPGDID
     GLVDCLVRLG TLLQDHPEIG EVDINPLLVG PDGCLALDAR IIPV
//
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