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Protein

Uracil phosphoribosyltransferase

Gene

upp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.

Catalytic activityi

UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP.

Enzyme regulationi

Allosterically activated by GTP.1 Publication

Kineticsi

  1. KM=0.53 µM for uracil1 Publication
  2. KM=58 µM for 5-phospho-alpha-D-ribose 1-diphosphate1 Publication

    Pathwayi: UMP biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes UMP from uracil.
    Proteins known to be involved in this subpathway in this organism are:
    1. Uracil phosphoribosyltransferase (upp)
    This subpathway is part of the pathway UMP biosynthesis via salvage pathway, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes UMP from uracil, the pathway UMP biosynthesis via salvage pathway and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei78 – 7815-phospho-alpha-D-ribose 1-diphosphateBy similarity
    Binding sitei103 – 10315-phospho-alpha-D-ribose 1-diphosphateBy similarity
    Binding sitei193 – 1931Uracil; via amide nitrogenBy similarity
    Binding sitei199 – 19915-phospho-alpha-D-ribose 1-diphosphateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    GTP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:URACIL-PRIBOSYLTRANS-MONOMER.
    ECOL316407:JW2483-MONOMER.
    MetaCyc:URACIL-PRIBOSYLTRANS-MONOMER.
    UniPathwayiUPA00574; UER00636.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uracil phosphoribosyltransferase (EC:2.4.2.9)
    Alternative name(s):
    UMP pyrophosphorylase
    UPRTase
    Gene namesi
    Name:upp
    Synonyms:uraP
    Ordered Locus Names:b2498, JW2483
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11332. upp.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311P → D: 60-fold reduction of the catalytic rate, and large decrease in uracil-binding affinity. 1 Publication

    Chemistry

    ChEMBLiCHEMBL2233621.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 208208Uracil phosphoribosyltransferasePRO_0000120824Add
    BLAST

    Proteomic databases

    EPDiP0A8F0.
    PaxDbiP0A8F0.
    PRIDEiP0A8F0.

    2D gel databases

    SWISS-2DPAGEP0A8F0.

    Expressioni

    Inductioni

    By pyrimidine starvation.

    Interactioni

    Subunit structurei

    Homodimer or homotrimer in the absence of substrates, and homopentamer or homohexamer in the presence of substrates.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-909572,EBI-909572

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4261438. 7 interactions.
    DIPiDIP-36228N.
    IntActiP0A8F0. 5 interactions.
    STRINGi511145.b2498.

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54Combined sources
    Helixi9 – 1911Combined sources
    Helixi25 – 4319Combined sources
    Turni44 – 463Combined sources
    Beta strandi49 – 568Combined sources
    Beta strandi59 – 668Combined sources
    Beta strandi72 – 765Combined sources
    Helixi79 – 835Combined sources
    Helixi84 – 907Combined sources
    Beta strandi98 – 1036Combined sources
    Turni105 – 1073Combined sources
    Beta strandi110 – 1167Combined sources
    Helixi121 – 1233Combined sources
    Beta strandi125 – 13511Combined sources
    Helixi137 – 14812Combined sources
    Beta strandi153 – 1619Combined sources
    Helixi163 – 17210Combined sources
    Beta strandi176 – 1816Combined sources
    Beta strandi185 – 1873Combined sources
    Beta strandi193 – 1953Combined sources
    Helixi200 – 2056Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EHJX-ray2.80A/B/C/D2-208[»]
    ProteinModelPortaliP0A8F0.
    SMRiP0A8F0. Positions 2-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8F0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni130 – 13895-phospho-alpha-D-ribose 1-diphosphate bindingBy similarity
    Regioni198 – 2003Uracil bindingBy similarity

    Sequence similaritiesi

    Belongs to the UPRTase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CZ5. Bacteria.
    COG0035. LUCA.
    HOGENOMiHOG000262754.
    InParanoidiP0A8F0.
    KOiK00761.
    OMAiVTVIDHP.
    PhylomeDBiP0A8F0.

    Family and domain databases

    CDDicd06223. PRTases_typeI. 1 hit.
    Gene3Di3.40.50.2020. 1 hit.
    HAMAPiMF_01218_B. Upp_B. 1 hit.
    InterProiIPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR005765. Ura_phspho_trans.
    [Graphical view]
    PfamiPF14681. UPRTase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01091. upp. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A8F0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIVEVKHPL VKHKLGLMRE QDISTKRFRE LASEVGSLLT YEATADLETE
    60 70 80 90 100
    KVTIEGWNGP VEIDQIKGKK ITVVPILRAG LGMMDGVLEN VPSARISVVG
    110 120 130 140 150
    MYRNEETLEP VPYFQKLVSN IDERMALIVD PMLATGGSVI ATIDLLKKAG
    160 170 180 190 200
    CSSIKVLVLV AAPEGIAALE KAHPDVELYT ASIDQGLNEH GYIIPGLGDA

    GDKIFGTK
    Length:208
    Mass (Da):22,533
    Last modified:June 7, 2005 - v1
    Checksum:iEF74D6E5B0216DC6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X57104 Genomic DNA. Translation: CAA40388.1.
    U00096 Genomic DNA. Translation: AAC75551.2.
    AP009048 Genomic DNA. Translation: BAA16386.1.
    PIRiA65026.
    RefSeqiNP_416993.2. NC_000913.3.
    WP_001295473.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75551; AAC75551; b2498.
    BAA16386; BAA16386; BAA16386.
    GeneIDi946979.
    KEGGiecj:JW2483.
    eco:b2498.
    PATRICi32120383. VBIEscCol129921_2594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X57104 Genomic DNA. Translation: CAA40388.1.
    U00096 Genomic DNA. Translation: AAC75551.2.
    AP009048 Genomic DNA. Translation: BAA16386.1.
    PIRiA65026.
    RefSeqiNP_416993.2. NC_000913.3.
    WP_001295473.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EHJX-ray2.80A/B/C/D2-208[»]
    ProteinModelPortaliP0A8F0.
    SMRiP0A8F0. Positions 2-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261438. 7 interactions.
    DIPiDIP-36228N.
    IntActiP0A8F0. 5 interactions.
    STRINGi511145.b2498.

    Chemistry

    ChEMBLiCHEMBL2233621.

    2D gel databases

    SWISS-2DPAGEP0A8F0.

    Proteomic databases

    EPDiP0A8F0.
    PaxDbiP0A8F0.
    PRIDEiP0A8F0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75551; AAC75551; b2498.
    BAA16386; BAA16386; BAA16386.
    GeneIDi946979.
    KEGGiecj:JW2483.
    eco:b2498.
    PATRICi32120383. VBIEscCol129921_2594.

    Organism-specific databases

    EchoBASEiEB1308.
    EcoGeneiEG11332. upp.

    Phylogenomic databases

    eggNOGiENOG4105CZ5. Bacteria.
    COG0035. LUCA.
    HOGENOMiHOG000262754.
    InParanoidiP0A8F0.
    KOiK00761.
    OMAiVTVIDHP.
    PhylomeDBiP0A8F0.

    Enzyme and pathway databases

    UniPathwayiUPA00574; UER00636.
    BioCyciEcoCyc:URACIL-PRIBOSYLTRANS-MONOMER.
    ECOL316407:JW2483-MONOMER.
    MetaCyc:URACIL-PRIBOSYLTRANS-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A8F0.
    PROiP0A8F0.

    Family and domain databases

    CDDicd06223. PRTases_typeI. 1 hit.
    Gene3Di3.40.50.2020. 1 hit.
    HAMAPiMF_01218_B. Upp_B. 1 hit.
    InterProiIPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR005765. Ura_phspho_trans.
    [Graphical view]
    PfamiPF14681. UPRTase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01091. upp. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiUPP_ECOLI
    AccessioniPrimary (citable) accession number: P0A8F0
    Secondary accession number(s): P25532, P78095, Q8XAC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: September 7, 2016
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.