RMLA2_SHIFL
ID RMLA2_SHIFL Reviewed; 293 AA.
AC P61888; P27831; P76755;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase 2 {ECO:0000250|UniProtKB:P61887};
DE EC=2.7.7.24 {ECO:0000250|UniProtKB:P61887};
DE AltName: Full=dTDP-glucose pyrophosphorylase 2 {ECO:0000250|UniProtKB:P61887};
DE AltName: Full=dTDP-glucose synthase 2 {ECO:0000250|UniProtKB:P61887};
GN Name=rffH; Synonyms=rmlA2; OrderedLocusNames=SF3863, S3897;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
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 [2]
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:P61887}.
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:P61887};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P61887};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P61887};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; dTDP-4-acetamido-4,6-
CC dideoxygalactose biosynthesis. {ECO:0000250|UniProtKB:P61887}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000250|UniProtKB:P61887}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P61887}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AE005674; AAN45300.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18898.1; -; Genomic_DNA.
DR RefSeq; NP_709593.1; NC_004337.2.
DR RefSeq; WP_000676056.1; NZ_WPGW01000028.1.
DR AlphaFoldDB; P61888; -.
DR SMR; P61888; -.
DR STRING; 198214.SF3863; -.
DR DrugBank; DB02452; Thymidine 5'-triphosphate.
DR EnsemblBacteria; AAN45300; AAN45300; SF3863.
DR EnsemblBacteria; AAP18898; AAP18898; S3897.
DR GeneID; 1025982; -.
DR GeneID; 66672308; -.
DR KEGG; sfl:SF3863; -.
DR KEGG; sfx:S3897; -.
DR PATRIC; fig|198214.7.peg.4553; -.
DR HOGENOM; CLU_029499_9_0_6; -.
DR OMA; ITHAIQW; -.
DR OrthoDB; 1004719at2; -.
DR UniPathway; UPA00566; -.
DR UniPathway; UPA00817; -.
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:0009246; P:enterobacterial common antigen 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 Exopolysaccharide synthesis; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..293
FT /note="Glucose-1-phosphate thymidylyltransferase 2"
FT /id="PRO_0000208000"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
SQ SEQUENCE 293 AA; 32734 MW; 5DA66676CD8F9139 CRC64;
MKGIILAGGS GTRLHPITRG VSKQLLPIYD KPMIYYPLSV LMLAGIREIL IITTPEDKGY
FQRLLGDGSE FGIQLEYAEQ PSPDGLAQAF IIGETFLNGE PSCLVLGDNI FFGQGFSPKL
RHVAARTEGA TVFGYQVMDP ERFGVVEFDD NFRAISLEEK PKQPKSNWAV TGLYFYDSKV
VEYAKQVKPS ERGELEITSI NQMYLEAGNL TVELLGRGFA WLDTGTHDSL IEASTFVQTV
EKRQGFKIAC LEEIAWRNGW LDDEGVKRAA SSLAKTGYGQ YLLELLRARP RQY
