ID   RMLA_SALAN              Reviewed;         292 AA.
AC   P55254;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Salmonella anatum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=58712;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M32 / Group E1;
RX   PubMed=1372579; DOI=10.1093/genetics/130.3.429;
RA   Wang L., Romana L.K., Reeves P.R.;
RT   "Molecular analysis of a Salmonella enterica group E1 rfb gene cluster: O
RT   antigen and the genetic basis of the major polymorphism.";
RL   Genetics 130:429-443(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M32 / Group E1;
RX   PubMed=7684736; DOI=10.1128/jb.175.11.3408-3413.1993;
RA   Liu D., Haase A.M., Lindqvist L., Lindberg A.A., Reeves P.R.;
RT   "Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica:
RT   identification and characterization of transferase genes of groups B, C2,
RT   and E1.";
RL   J. Bacteriol. 175:3408-3413(1993).
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   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; X60665; CAA43074.1; -; Genomic_DNA.
DR   PIR; S23342; S23342.
DR   RefSeq; WP_023243995.1; NZ_WHYQ01000001.1.
DR   AlphaFoldDB; P55254; -.
DR   SMR; P55254; -.
DR   PATRIC; fig|58712.10.peg.2179; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
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:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0009243; P:O antigen 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   Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..292
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000207994"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  32441 MW;  00E6484705A66DEE CRC64;
     MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD
     TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI GNDDCALVLG DNIFYGHDLP
     KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDQSGTAVSL EEKPLQPKSN YAVTGLYFYD
     NSVVEMAKNL KPSARGELEI TDINRIYMEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI
     ATIEERQGLK VSCPEEIAYR KGFIDAEQIK NLAKPLSKNA YGQYLLNMIK GY