ID   RMLA_NEIMA              Reviewed;         288 AA.
AC   P57040; A1IP45;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=rmlA1; Synonyms=rfbA1; OrderedLocusNames=NMA0188;
GN   and
GN   Name=rmlA2; Synonyms=rfbA2; OrderedLocusNames=NMA0205;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07503.1; -; Genomic_DNA.
DR   EMBL; AL157959; CAM07519.1; -; Genomic_DNA.
DR   PIR; H82014; H82014.
DR   RefSeq; WP_010981057.1; NC_003116.1.
DR   AlphaFoldDB; P57040; -.
DR   SMR; P57040; -.
DR   EnsemblBacteria; CAM07503; CAM07503; NMA0188.
DR   EnsemblBacteria; CAM07519; CAM07519; NMA0205.
DR   KEGG; nma:NMA0188; -.
DR   KEGG; nma:NMA0205; -.
DR   HOGENOM; CLU_029499_9_0_4; -.
DR   OMA; FTWLDTG; -.
DR   BioCyc; NMEN122587:NMA_RS00970-MON; -.
DR   BioCyc; NMEN122587:NMA_RS01055-MON; -.
DR   Proteomes; UP000000626; 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: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_0000207997"
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;  32152 MW;  C818727C546F5E00 CRC64;
     MKGIILAGGS GTRLYPITRG VSKQLLPVYD KPMIYYPLSV LMLAGIRDIL VITAPEDNAS
     FKRLLGDGSD FGISISYAVQ PSPDGLAQAF IIGEEFIGND NVCLVLGDNI FYGQSFTQTL
     KQAAAQTHGA TVFAYQVKNP ERFGVVEFNE NFRAVSIEEK PQRPKSDWAV TGLYFYDNRA
     VEFAKQLKPS ARGELEISDL NRMYLEDGSL SVQILGRGFA WLDTGTHESL HEAASFVQTV
     QNIQNLHIAC LEEIAWRNGW LSDEKLEELA RTMAKNQYGQ YLLRLLKK