ID   CITG_STRMU              Reviewed;         296 AA.
AC   Q8DUC9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE            Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00397};
DE            EC=2.4.2.52 {ECO:0000255|HAMAP-Rule:MF_00397};
GN   Name=citG {ECO:0000255|HAMAP-Rule:MF_00397}; OrderedLocusNames=SMU_1011;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)-
CC         3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00397};
CC   -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00397}.
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DR   EMBL; AE014133; AAN58712.1; -; Genomic_DNA.
DR   RefSeq; NP_721406.1; NC_004350.2.
DR   RefSeq; WP_002263234.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUC9; -.
DR   STRING; 210007.SMU_1011; -.
DR   PRIDE; Q8DUC9; -.
DR   EnsemblBacteria; AAN58712; AAN58712; SMU_1011.
DR   KEGG; smu:SMU_1011; -.
DR   PATRIC; fig|210007.7.peg.904; -.
DR   eggNOG; COG1767; Bacteria.
DR   HOGENOM; CLU_056179_1_0_9; -.
DR   OMA; QSWQRPA; -.
DR   PhylomeDB; Q8DUC9; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   HAMAP; MF_00397; CitG; 1.
DR   InterPro; IPR002736; CitG.
DR   InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG.
DR   PANTHER; PTHR30201; PTHR30201; 1.
DR   Pfam; PF01874; CitG; 1.
DR   TIGRFAMs; TIGR03125; citrate_citG; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..296
FT                   /note="Probable 2-(5''-triphosphoribosyl)-3'-
FT                   dephosphocoenzyme-A synthase"
FT                   /id="PRO_0000214676"
SQ   SEQUENCE   296 AA;  33941 MW;  040CDBF6C22F5914 CRC64;
     MQTKEKLASL SYLAVKSLLY ELNLTPKPGL VDCHNNGAHN DMDFYTFLDS ILSLSPFFKK
     YIEVGWLYHN ESPQYLFNQL RKLGIEAEAA MFSATERVNT HKGINFSFAL LLGATGSYLA
     KHIELIQEKR RFMPQDSLTI CHLAGEMSMH LIQNDLSHVE TKRNLTYGEK LFLQYGLKGL
     RGEASQGYPS LTQKALPFFR NELLKKQDIQ ISQLKLLLYL MTFIEDSNII HRGGIKSWKK
     VQQEAQTLLE KDLPPYQLKE QLNSYNQILT DRHLSPGGAA DLLSLTLYFS FLEQLI