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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: dTDP-L-rhamnose biosynthesis

    This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

    Pathwayi: LPS O-antigen biosynthesis

    This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.
    View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi111MagnesiumBy similarity1
    Metal bindingi226MagnesiumBy similarity1

    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

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi201T → A: Two-fold increase in the conversion of 2-acetamido-2-deoxy-alpha-D-glucopyranosyl phosphate. 1 Publication1
    Mutagenesisi224W → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002079951 – 292Glucose-1-phosphate thymidylyltransferaseAdd BLAST292

    Proteomic databases

    PaxDbiP26393.
    PRIDEiP26393.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi99287.STM2095.

    Structurei

    Secondary structure

    1292
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Helixi15 – 17Combined sources3
    Helixi20 – 22Combined sources3
    Helixi26 – 28Combined sources3
    Beta strandi29 – 31Combined sources3
    Helixi38 – 46Combined sources9
    Beta strandi51 – 56Combined sources6
    Turni58 – 60Combined sources3
    Helixi61 – 68Combined sources8
    Helixi72 – 74Combined sources3
    Beta strandi77 – 82Combined sources6
    Beta strandi84 – 87Combined sources4
    Helixi89 – 91Combined sources3
    Helixi92 – 95Combined sources4
    Helixi97 – 100Combined sources4
    Beta strandi105 – 109Combined sources5
    Beta strandi112 – 115Combined sources4
    Helixi119 – 128Combined sources10
    Beta strandi131 – 139Combined sources9
    Helixi143 – 145Combined sources3
    Beta strandi146 – 151Combined sources6
    Beta strandi153 – 155Combined sources3
    Beta strandi157 – 163Combined sources7
    Beta strandi168 – 179Combined sources12
    Helixi183 – 189Combined sources7
    Helixi200 – 209Combined sources10
    Beta strandi213 – 217Combined sources5
    Beta strandi222 – 226Combined sources5
    Helixi230 – 247Combined sources18
    Helixi254 – 260Combined sources7
    Helixi266 – 273Combined sources8
    Helixi274 – 276Combined sources3
    Helixi280 – 288Combined sources9

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP26393.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4108I19. Bacteria.
    COG1209. LUCA.
    HOGENOMiHOG000283473.
    KOiK00973.
    OMAiPHDAEQF.
    PhylomeDBiP26393.

    Family and domain databases

    CDDicd02538. G1P_TT_short. 1 hit.
    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR005907. G1P_thy_trans_s.
    IPR005835. NTP_transferase_dom.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR22572:SF105. PTHR22572:SF105. 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
    PDB 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.
    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

    eggNOGiENOG4108I19. Bacteria.
    COG1209. LUCA.
    HOGENOMiHOG000283473.
    KOiK00973.
    OMAiPHDAEQF.
    PhylomeDBiP26393.

    Enzyme and pathway databases

    UniPathwayiUPA00124.
    UPA00281.
    SABIO-RKP26393.

    Miscellaneous databases

    EvolutionaryTraceiP26393.

    Family and domain databases

    CDDicd02538. G1P_TT_short. 1 hit.
    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR005907. G1P_thy_trans_s.
    IPR005835. NTP_transferase_dom.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR22572:SF105. PTHR22572:SF105. 1 hit.
    PfamiPF00483. NTP_transferase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.
    TIGRFAMsiTIGR01207. rmlA. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 118 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

    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 one 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.