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P26393

- RMLA_SALTY

UniProt

P26393 - RMLA_SALTY

Protein

Glucose-1-phosphate thymidylyltransferase

Gene

rmlA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    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.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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 110 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