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Protein

Glucose-1-phosphate thymidylyltransferase

Gene

rmlA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: 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

Mg2+CuratedNote: Binds 1 Mg2+ ion per subunit.Curated

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 – 1111MagnesiumBy similarity
    Metal bindingi226 – 2261MagnesiumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    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 Componenti: 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 – 95Combined sources
    Helixi15 – 173Combined sources
    Helixi20 – 223Combined sources
    Helixi26 – 283Combined sources
    Beta strandi29 – 313Combined sources
    Helixi38 – 469Combined sources
    Beta strandi51 – 566Combined sources
    Turni58 – 603Combined sources
    Helixi61 – 688Combined sources
    Helixi72 – 743Combined sources
    Beta strandi77 – 826Combined sources
    Beta strandi84 – 874Combined sources
    Helixi89 – 913Combined sources
    Helixi92 – 954Combined sources
    Helixi97 – 1004Combined sources
    Beta strandi105 – 1095Combined sources
    Beta strandi112 – 1154Combined sources
    Helixi119 – 12810Combined sources
    Beta strandi131 – 1399Combined sources
    Helixi143 – 1453Combined sources
    Beta strandi146 – 1516Combined sources
    Beta strandi153 – 1553Combined sources
    Beta strandi157 – 1637Combined sources
    Beta strandi168 – 17912Combined sources
    Helixi183 – 1897Combined sources
    Helixi200 – 20910Combined sources
    Beta strandi213 – 2175Combined sources
    Beta strandi222 – 2265Combined sources
    Helixi230 – 24718Combined sources
    Helixi254 – 2607Combined sources
    Helixi266 – 2738Combined sources
    Helixi274 – 2763Combined sources
    Helixi280 – 2889Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26393.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1209.
    HOGENOMiHOG000283473.
    KOiK00973.
    OMAiPHDAEQF.
    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

            10         20         30         40         50
    MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR
    60 70 80 90 100
    DILIISTPQD TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI
    110 120 130 140 150
    GHDDCALVLG DNIFYGHDLP KLMEAAVNKE SGATVFAYHV NDPERYGVVE
    160 170 180 190 200
    FDQKGTAVSL EEKPLQPKSN YAVTGLYFYD NSVVEMAKNL KPSARGELEI
    210 220 230 240 250
    TDINRIYMEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI ATIEERQGLK
    260 270 280 290
    VSCPEEIAFR KNFINAQQVI ELAGPLSKND YGKYLLKMVK GL
    Length:292
    Mass (Da):32,453
    Last modified:August 1, 1992 - v1
    Checksum:i11065BA9DF2B0268
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM2095.

    Proteomic databases

    PaxDbiP26393.
    PRIDEiP26393.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG1209.
    HOGENOMiHOG000283473.
    KOiK00973.
    OMAiPHDAEQF.
    OrthoDBiEOG6RC3RN.
    PhylomeDBiP26393.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP26393.

    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.
    ProtoNetiSearch...

    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: January 7, 2015
    This is version 112 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.Curated

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.