RMLA1_SHIFL
ID RMLA1_SHIFL Reviewed; 292 AA.
AC P37779; Q54164;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase 1 {ECO:0000250|UniProtKB:P37744};
DE EC=2.7.7.24 {ECO:0000250|UniProtKB:P37744};
DE AltName: Full=dTDP-glucose pyrophosphorylase 1 {ECO:0000250|UniProtKB:P37744};
DE AltName: Full=dTDP-glucose synthase 1 {ECO:0000250|UniProtKB:P37744};
GN Name=rfbA; Synonyms=rmlA1; OrderedLocusNames=SF2102, S2225;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=8170390; DOI=10.1111/j.1365-2958.1994.tb00308.x;
RA Macpherson D.F., Manning P.A., Morona R.;
RT "Characterization of the dTDP-rhamnose biosynthetic genes encoded in the
RT rfb locus of Shigella flexneri.";
RL Mol. Microbiol. 11:281-292(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6200 / Serotype 2a;
RX PubMed=8157605; DOI=10.1128/jb.176.8.2362-2373.1994;
RA Rajakumar K., Jost B.H., Sasakawa C., Okada N., Yoshikawa M., Adler B.;
RT "Nucleotide sequence of the rhamnose biosynthetic operon of Shigella
RT flexneri 2a and role of lipopolysaccharide in virulence.";
RL J. Bacteriol. 176:2362-2373(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000250|UniProtKB:P37744}.
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 Evidence={ECO:0000250|UniProtKB:P37744};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P37744};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P37744};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000250|UniProtKB:P37744}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000250|UniProtKB:P37744}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P37744}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; X71970; CAA50769.1; -; Genomic_DNA.
DR EMBL; L14842; AAA53681.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN43641.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17470.1; -; Genomic_DNA.
DR PIR; S41536; S41536.
DR RefSeq; NP_707934.1; NC_004337.2.
DR RefSeq; WP_000857518.1; NZ_WPGW01000076.1.
DR AlphaFoldDB; P37779; -.
DR SMR; P37779; -.
DR STRING; 198214.SF2102; -.
DR PRIDE; P37779; -.
DR EnsemblBacteria; AAN43641; AAN43641; SF2102.
DR EnsemblBacteria; AAP17470; AAP17470; S2225.
DR GeneID; 1025289; -.
DR KEGG; sfl:SF2102; -.
DR KEGG; sft:NCTC1_02310; -.
DR KEGG; sfx:S2225; -.
DR PATRIC; fig|198214.7.peg.2510; -.
DR HOGENOM; CLU_029499_9_0_6; -.
DR OMA; PFIMYLG; -.
DR OrthoDB; 1004719at2; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; Transferase.
FT CHAIN 1..292
FT /note="Glucose-1-phosphate thymidylyltransferase 1"
FT /id="PRO_0000207999"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
FT CONFLICT 157
FT /note="A -> P (in Ref. 1; CAA50769)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> Q (in Ref. 1; CAA50769)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="Missing (in Ref. 1; CAA50769)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="W -> C (in Ref. 1; CAA50769)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..233
FT /note="GTHQSL -> DTSKP (in Ref. 1; CAA50769)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..245
FT /note="IEE -> NED (in Ref. 1; CAA50769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 32487 MW; E54F6199E0361AF2 CRC64;
MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD
TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI GGDDCALVLG DNIFYGHDLP
KLMDTAVNRE SGATVFAYHV NDPERYGVVE FDDNGTAISL EEKPQEPKSN YAVTGLYFYD
NDVVEMAKNL KPSARGELEI TDINRIYMDQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI
ATIEERQGLK VSCPEEIAHR KGFIDAEQVK VLAEPLKKNA YGQYLLKMIK GY
