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 27-MAR-2024, entry version 126.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE EC=2.7.7.24 {ECO:0000250|UniProtKB:P61887};
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; Bacillota; 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 Evidence={ECO:0000250|UniProtKB:P61887};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P61887};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P61887};
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 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 OrthoDB; 9803871at2; -.
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 InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01207; rmlA; 1.
DR PANTHER; PTHR43532; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43532:SF1; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 1; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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|UniProtKB:P61887"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
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
//
