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P26393

- RMLA_SALTY

UniProt

P26393 - RMLA_SALTY

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Protein

Glucose-1-phosphate thymidylyltransferase

Gene
rmlA, rfbA, STM2095
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit Inferred.

Kineticsi

  1. KM=0.7 mM for dTTP
  2. KM=0.3 mM for G1P

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111Magnesium By similarity
Metal bindingi226 – 2261Magnesium By similarity

GO - Molecular functioni

  1. glucose-1-phosphate thymidylyltransferase activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB

GO - Biological processi

  1. dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  2. extracellular polysaccharide biosynthetic process Source: UniProtKB
  3. O antigen biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2107-MONOMER.
SABIO-RKP26393.
UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-1-phosphate thymidylyltransferase (EC:2.7.7.24)
Alternative name(s):
dTDP-glucose pyrophosphorylase
Short name:
Ep
dTDP-glucose synthase
Gene namesi
Name:rmlA
Synonyms:rfbA
Ordered Locus Names:STM2095
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011T → A: Two-fold increase in the conversion of 2-acetamido-2-deoxy-alpha-D-glucopyranosyl phosphate. 1 Publication
Mutagenesisi224 – 2241W → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Glucose-1-phosphate thymidylyltransferasePRO_0000207995Add
BLAST

Proteomic databases

PaxDbiP26393.
PRIDEiP26393.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi99287.STM2095.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95
Helixi15 – 173
Helixi20 – 223
Helixi26 – 283
Beta strandi29 – 313
Helixi38 – 469
Beta strandi51 – 566
Turni58 – 603
Helixi61 – 688
Helixi72 – 743
Beta strandi77 – 826
Beta strandi84 – 874
Helixi89 – 913
Helixi92 – 954
Helixi97 – 1004
Beta strandi105 – 1095
Beta strandi112 – 1154
Helixi119 – 12810
Beta strandi131 – 1399
Helixi143 – 1453
Beta strandi146 – 1516
Beta strandi153 – 1553
Beta strandi157 – 1637
Beta strandi168 – 17912
Helixi183 – 1897
Helixi200 – 20910
Beta strandi213 – 2175
Beta strandi222 – 2265
Helixi230 – 24718
Helixi254 – 2607
Helixi266 – 2738
Helixi274 – 2763
Helixi280 – 2889

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP26393.
SMRiP26393. Positions 1-289.

Miscellaneous databases

EvolutionaryTraceiP26393.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1209.
HOGENOMiHOG000283473.
KOiK00973.
OMAiWITRDEL.
OrthoDBiEOG6RC3RN.
PhylomeDBiP26393.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005907. G1P_thy_trans_s.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22572:SF13. PTHR22572:SF13. 1 hit.
PfamiPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01207. rmlA. 1 hit.

Sequencei

Sequence statusi: Complete.

P26393-1 [UniParc]FASTAAdd to Basket

« Hide

MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR    50
DILIISTPQD TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI 100
GHDDCALVLG DNIFYGHDLP KLMEAAVNKE SGATVFAYHV NDPERYGVVE 150
FDQKGTAVSL EEKPLQPKSN YAVTGLYFYD NSVVEMAKNL KPSARGELEI 200
TDINRIYMEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI ATIEERQGLK 250
VSCPEEIAFR KNFINAQQVI ELAGPLSKND YGKYLLKMVK GL 292
Length:292
Mass (Da):32,453
Last modified:August 1, 1992 - v1
Checksum:i11065BA9DF2B0268
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56793 Genomic DNA. Translation: CAA40117.1.
AE006468 Genomic DNA. Translation: AAL20999.1.
PIRiS15301.
RefSeqiNP_461040.1. NC_003197.1.
WP_000857529.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20999; AAL20999; STM2095.
GeneIDi1253616.
KEGGistm:STM2095.
PATRICi32382773. VBISalEnt20916_2217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56793 Genomic DNA. Translation: CAA40117.1 .
AE006468 Genomic DNA. Translation: AAL20999.1 .
PIRi S15301.
RefSeqi NP_461040.1. NC_003197.1.
WP_000857529.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IIM X-ray 2.10 A/B 1-292 [» ]
1IIN X-ray 2.10 A/B/C/D 1-292 [» ]
1MP3 X-ray 2.20 A/B 1-292 [» ]
1MP4 X-ray 2.20 A/B 1-292 [» ]
1MP5 X-ray 2.75 A/B/C/D 1-292 [» ]
3PKP X-ray 2.60 A/B/C/D/I/J/K/L 1-292 [» ]
3PKQ X-ray 2.40 A/B/C/D 1-292 [» ]
ProteinModelPortali P26393.
SMRi P26393. Positions 1-289.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM2095.

Proteomic databases

PaxDbi P26393.
PRIDEi P26393.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20999 ; AAL20999 ; STM2095 .
GeneIDi 1253616.
KEGGi stm:STM2095.
PATRICi 32382773. VBISalEnt20916_2217.

Phylogenomic databases

eggNOGi COG1209.
HOGENOMi HOG000283473.
KOi K00973.
OMAi WITRDEL.
OrthoDBi EOG6RC3RN.
PhylomeDBi P26393.

Enzyme and pathway databases

UniPathwayi UPA00124 .
UPA00281 .
BioCyci SENT99287:GCTI-2107-MONOMER.
SABIO-RK P26393.

Miscellaneous databases

EvolutionaryTracei P26393.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR005907. G1P_thy_trans_s.
IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR22572:SF13. PTHR22572:SF13. 1 hit.
Pfami PF00483. NTP_transferase. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01207. rmlA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiRMLA_SALTY
AccessioniPrimary (citable) accession number: P26393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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