ID   RMLA_STRGR              Reviewed;         355 AA.
AC   P08075;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE            EC=2.7.7.24;
DE   AltName: Full=Sugar-nucleotidylation enzyme;
DE   AltName: Full=dTDP-glucose pyrophosphorylase;
DE   AltName: Full=dTDP-glucose synthase;
GN   Name=strD;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N2-3-11;
RX   PubMed=3118332; DOI=10.1093/nar/15.19.8041;
RA   Distler J., Ebert A., Mansouri K., Pissowotzki K., Stockmann M.,
RA   Piepersberg W.;
RT   "Gene cluster for streptomycin biosynthesis in Streptomyces griseus:
RT   nucleotide sequence of three genes and analysis of transcriptional
RT   activity.";
RL   Nucleic Acids Res. 15:8041-8056(1987).
CC   -!- FUNCTION: Involved in the biosynthesis of the streptose moiety of
CC       streptomycin. Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis (By similarity).
CC       {ECO:0000250}.
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: Antibiotic biosynthesis; streptomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; Y00459; CAA68514.1; -; Genomic_DNA.
DR   PIR; A26984; A26984.
DR   AlphaFoldDB; P08075; -.
DR   SMR; P08075; -.
DR   PRIDE; P08075; -.
DR   UniPathway; UPA00066; -.
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:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04189; G1P_TT_long; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005908; G1P_thy_trans_l.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01208; rmlA_long; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Streptomycin biosynthesis; Transferase.
FT   CHAIN           1..355
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000208005"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  38098 MW;  ED136AEA854EB7DA CRC64;
     MKALVLAGGT GTRLRPITHT SAKQLVPVAN KPVLFYGLEA IRAAGIIDVG IVVGDTADEI
     VAAVGDGSRF GLKVSYIPQS KPLGLAHCVL ISRDFLGEDD FIMYLGDNFV VGVVEDSVRE
     FRAARPDAHL MLTRVPEPRS FGVAELSDSG QVLGLEEKPA HPKSDLALVG VYLFSPAIHE
     AVAAITPSWR GELEITDAVQ WLIDAGRDVR STVISGYWKD TGNVTDMLEV NRLVLETTEP
     RCDGLVDERS DLIGRVLVEE GAEVRNSRVM GPTVIGAGTR VTNSYVGPFT SLAEDCVVED
     SEVEFSIVLR GASISGVRRI EASLIGRHVQ VTSAPEVPHA NRLVLGDHSR AQISS