ID   RMLA_STRMU              Reviewed;         289 AA.
AC   P95778;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE            EC=2.7.7.24;
DE   AltName: Full=dTDP-glucose pyrophosphorylase;
DE   AltName: Full=dTDP-glucose synthase;
GN   Name=rmlA; OrderedLocusNames=SMU_1461;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Xc / Serotype c;
RX   PubMed=9023194; DOI=10.1128/jb.179.4.1126-1134.1997;
RA   Tsukioka Y., Yamashita Y., Oho T., Nakano Y., Koga T.;
RT   "Biological function of the dTDP-rhamnose synthesis pathway in
RT   Streptococcus mutans.";
RL   J. Bacteriol. 179:1126-1134(1997).
RN   [2]
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   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis.
CC       {ECO:0000269|PubMed:9023194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC         dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:58601; EC=2.7.7.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; D78182; BAA11247.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59119.1; -; Genomic_DNA.
DR   RefSeq; NP_721813.1; NC_004350.2.
DR   RefSeq; WP_002263084.1; NC_004350.2.
DR   AlphaFoldDB; P95778; -.
DR   SMR; P95778; -.
DR   STRING; 210007.SMU_1461; -.
DR   PRIDE; P95778; -.
DR   EnsemblBacteria; AAN59119; AAN59119; SMU_1461.
DR   GeneID; 66819137; -.
DR   KEGG; smu:SMU_1461; -.
DR   PATRIC; fig|210007.7.peg.1299; -.
DR   eggNOG; COG1209; Bacteria.
DR   HOGENOM; CLU_029499_9_0_9; -.
DR   OMA; FTWLDTG; -.
DR   PhylomeDB; P95778; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02538; G1P_TT_short; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005907; G1P_thy_trans_s.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43532; PTHR43532; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01207; rmlA; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..289
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000208004"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32295 MW;  5563650C07C00987 CRC64;
     MKGIILAGGS GTRLYPLTRA ASKQLMPVYD KPMIYYPLST LMLAGIKDIL IISTPQDLPR
     FKELLQDGSE FGIKLSYAEQ PSPDGLAQAF IIGEEFIGDD HVALILGDNI YYGPGLSRML
     QKAASKESGA TVFGYQVKDP ERFGVVEFDN DRNAISIEEK PEHPKSHYAV TGLYFYDNSV
     VDIAKNIKPS PRGELEITDV NKAYLDRGDL SVEVMERGFA WLDTGTHESL LEAAQYIETV
     QRMQNLQVAN LEEIAYRMGY ITADQVRELA QPLKKNEYGQ YLLRLIGEA