ID   RMLA_MYCTO              Reviewed;         288 AA.
AC   P9WH12; L0T524; P72017; Q797X3; Q7DA01;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
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; OrderedLocusNames=MT0348;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis. Involved in the
CC       biosynthesis of the dTDP-L-rhamnose which is a component of the
CC       critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which
CC       connects the galactan region of arabinogalactan to peptidoglycan via a
CC       phosphodiester linkage (By similarity). {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   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44571.1; -; Genomic_DNA.
DR   PIR; G70527; G70527.
DR   RefSeq; WP_003401670.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WH12; -.
DR   SMR; P9WH12; -.
DR   EnsemblBacteria; AAK44571; AAK44571; MT0348.
DR   GeneID; 45424301; -.
DR   KEGG; mtc:MT0348; -.
DR   PATRIC; fig|83331.31.peg.369; -.
DR   HOGENOM; CLU_029499_9_0_11; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000001020; 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   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_0000428267"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  31492 MW;  90873DE4C76E930C CRC64;
     MRGIILAGGS GTRLYPITMG ISKQLLPVYD KPMIYYPLTT LMMAGIRDIQ LITTPHDAPG
     FHRLLGDGAH LGVNISYATQ DQPDGLAQAF VIGANHIGAD SVALVLGDNI FYGPGLGTSL
     KRFQSISGGA IFAYWVANPS AYGVVEFGAE GMALSLEEKP VTPKSNYAVP GLYFYDNDVI
     EIARGLKKSA RGEYEITEVN QVYLNQGRLA VEVLARGTAW LDTGTFDSLL DAADFVRTLE
     RRQGLKVSIP EEVAWRMGWI DDEQLVQRAR ALVKSGYGNY LLELLERN