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P26393 (RMLA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-1-phosphate thymidylyltransferase

EC=2.7.7.24
Alternative name(s):
dTDP-glucose pyrophosphorylase
Short name=Ep
dTDP-glucose synthase
Gene names
Name:rmlA
Synonyms:rfbA
Ordered Locus Names:STM2095
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars. Ref.3

Catalytic activity

dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose.

Cofactor

Binds 1 magnesium ion per subunit Probable.

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the glucose-1-phosphate thymidylyltransferase family.

Caution

The position of the magnesium ion observed in the crystallographic structure is different from that observed in the structure of E.coli RmlA2 (RffH) and does not seem to correspond to the binding site for the catalytically essential magnesium ion. Therefore, we choose to propagate in the feature lines the positions found in the E.coli structure.

Biophysicochemical properties

Kinetic parameters:

KM=0.7 mM for dTTP

KM=0.3 mM for G1P

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Glucose-1-phosphate thymidylyltransferase
PRO_0000207995

Sites

Metal binding1111Magnesium By similarity
Metal binding2261Magnesium By similarity

Experimental info

Mutagenesis2011T → A: Two-fold increase in the conversion of 2-acetamido-2-deoxy-alpha-D-glucopyranosyl phosphate. Ref.4
Mutagenesis2241W → H: Is able to convert both 6-acetamido-6-deoxy-alpha-D-glucopyranosyl phosphate and alpha-D-glucopyranuronic acid 1-(dihydrogen phosphate), which are not accepted by the wild-type. Ref.4

Secondary structure

.............................................................. 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26393 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 11065BA9DF2B0268

FASTA29232,453
        10         20         30         40         50         60 
MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD 

        70         80         90        100        110        120 
TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI GHDDCALVLG DNIFYGHDLP 

       130        140        150        160        170        180 
KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDQKGTAVSL EEKPLQPKSN YAVTGLYFYD 

       190        200        210        220        230        240 
NSVVEMAKNL KPSARGELEI TDINRIYMEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI 

       250        260        270        280        290 
ATIEERQGLK VSCPEEIAFR KNFINAQQVI ELAGPLSKND YGKYLLKMVK GL 

« Hide

References

« Hide 'large scale' references
[1]"Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)."
Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.
Mol. Microbiol. 5:695-713(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Purification, characterization and HPLC assay of Salmonella glucose-1-phosphate thymidylyltransferase from the cloned rfbA gene."
Lindquist L., Kaiser R., Reeves P.R., Lindberg A.A.
Eur. J. Biochem. 211:763-770(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22, FUNCTION.
Strain: LT2.
[4]"Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization."
Barton W.A., Lesniak J., Biggins J.B., Jeffrey P.D., Jiang J., Rajashankar K.R., Thorson J.S., Nikolov D.B.
Nat. Struct. Biol. 8:545-551(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF THR-201 AND TRP-224, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF COMPLEXES WITH UDP-GLC AND DTTP.
Strain: LT2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56793 Genomic DNA. Translation: CAA40117.1.
AE006468 Genomic DNA. Translation: AAL20999.1.
PIRS15301.
RefSeqNP_461040.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IIMX-ray2.10A/B1-292[»]
1IINX-ray2.10A/B/C/D1-292[»]
1MP3X-ray2.20A/B1-292[»]
1MP4X-ray2.20A/B1-292[»]
1MP5X-ray2.75A/B/C/D1-292[»]
3PKPX-ray2.60A/B/C/D/I/J/K/L1-292[»]
3PKQX-ray2.40A/B/C/D1-292[»]
ProteinModelPortalP26393.
SMRP26393. Positions 1-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2095.

Proteomic databases

PaxDbP26393.
PRIDEP26393.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20999; AAL20999; STM2095.
GeneID1253616.
KEGGstm:STM2095.
PATRIC32382773. VBISalEnt20916_2217.

Phylogenomic databases

eggNOGCOG1209.
HOGENOMHOG000283473.
KOK00973.
OMAWITRDEL.
OrthoDBEOG6RC3RN.
PhylomeDBP26393.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2107-MONOMER.
SABIO-RKP26393.
UniPathwayUPA00124.
UPA00281.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR005907. G1P_thy_trans_s.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR22572:SF13. PTHR22572:SF13. 1 hit.
PfamPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01207. rmlA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP26393.

Entry information

Entry nameRMLA_SALTY
AccessionPrimary (citable) accession number: P26393
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways