ID   RMLA_XANCB              Reviewed;         295 AA.
AC   B0RVK9; P55256;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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; OrderedLocusNames=xcc-b100_3733;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8253667; DOI=10.1128/jb.175.24.7786-7792.1993;
RA   Koeplin R., Wang G., Hoette B., Priefer U.B., Puehler A.;
RT   "A 3.9-kb DNA region of Xanthomonas campestris pv. campestris that is
RT   necessary for lipopolysaccharide production encodes a set of enzymes
RT   involved in the synthesis of dTDP-rhamnose.";
RL   J. Bacteriol. 175:7786-7792(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AF204145; AAA16191.1; -; Genomic_DNA.
DR   EMBL; AM920689; CAP53100.1; -; Genomic_DNA.
DR   PIR; A49906; A49906.
DR   AlphaFoldDB; B0RVK9; -.
DR   SMR; B0RVK9; -.
DR   KEGG; xca:xcc-b100_3733; -.
DR   HOGENOM; CLU_029499_9_0_6; -.
DR   OMA; PFIMYLG; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000001188; 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: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..295
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000333188"
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   295 AA;  32508 MW;  585D239B6EAF4554 CRC64;
     MTQRKGIILA GGSGTRLYPI TKGVSKQLLP VYDKPMIYYP LSVLMLAGIR DILIINTPHE
     QALFQSLLGD GAQWGVNIQY AVQPSPDGLA QAYLIGRDFV GGKPSCLVLG DNIFHGHGLT
     DTLRRADARE QGATVFGYWV NDPERYGVAE FDQHGKVIDI AEKPEKPRSN YAVTGLYFYD
     GKASDYAAAL KPSPRGELEI TDLNRCYLDA GDLHLEPLGR GYAWLDTGTH QSLHEAANFI
     ETIQMRQGLQ VCCPEEIAFG QGWIDAEQLE RLAAPLLKND YGKYLTALAK RGAVH