ID   RMLA_NEIGO              Reviewed;         288 AA.
AC   P37762;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 74.
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; Synonyms=rfbA;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=7961452; DOI=10.1128/jb.176.22.6915-6920.1994;
RA   Robertson B.D., Frosch M., van Putten J.P.M.;
RT   "The identification of cryptic rhamnose biosynthesis genes in Neisseria
RT   gonorrhoeae and their relationship to lipopolysaccharide biosynthesis.";
RL   J. Bacteriol. 176:6915-6920(1994).
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis. {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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; Z32742; CAA83653.1; -; Genomic_DNA.
DR   EMBL; Z21508; CAA79719.1; -; Genomic_DNA.
DR   PIR; S47046; S47046.
DR   RefSeq; WP_017147193.1; NZ_RJZD01000019.1.
DR   AlphaFoldDB; P37762; -.
DR   SMR; P37762; -.
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:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
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   Magnesium; Metal-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..288
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000207996"
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   288 AA;  32029 MW;  1FD877B65B667EA4 CRC64;
     MKGIILAGGS GTRLYPITRG VSKQLLPVYD KPMIYYPLSV LMLAGIRDIL VITAPEDNAA
     FQRLLGDGSD FGIRLQYAVQ PSPDGLAQAF IIGEEFIGNG NVCLILGDNI FYGQSFTQTL
     KQAAAKTHGA TVFGYRVKDP ERFGVVEFDE NFNALSIEEK PQQPKSDWAV TGLYFHDNRA
     VEFAKQLKPS ARGELEISDL NRMYLEDGSL SVQILGRGFA WLDTGTQESL HEAASFVQTV
     QNIQNLHIAC LEEIAWRNGW LTKKDVETRA KHLEKTAYGQ YLLHLIGK