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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)DescriptionActionsGraphical viewLength
    Binding sitei785-phospho-alpha-D-ribose 1-diphosphateBy similarity1
    Binding sitei1035-phospho-alpha-D-ribose 1-diphosphateBy similarity1
    Binding sitei193Uracil; via amide nitrogenBy similarity1
    Binding sitei1995-phospho-alpha-D-ribose 1-diphosphateBy similarity1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi131P → D: 60-fold reduction of the catalytic rate, and large decrease in uracil-binding affinity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL2233621.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001208241 – 208Uracil phosphoribosyltransferaseAdd BLAST208

    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 interactors.
    DIPiDIP-36228N.
    IntActiP0A8F0. 5 interactors.
    STRINGi511145.b2498.

    Structurei

    Secondary structure

    1208
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 5Combined sources4
    Helixi9 – 19Combined sources11
    Helixi25 – 43Combined sources19
    Turni44 – 46Combined sources3
    Beta strandi49 – 56Combined sources8
    Beta strandi59 – 66Combined sources8
    Beta strandi72 – 76Combined sources5
    Helixi79 – 83Combined sources5
    Helixi84 – 90Combined sources7
    Beta strandi98 – 103Combined sources6
    Turni105 – 107Combined sources3
    Beta strandi110 – 116Combined sources7
    Helixi121 – 123Combined sources3
    Beta strandi125 – 135Combined sources11
    Helixi137 – 148Combined sources12
    Beta strandi153 – 161Combined sources9
    Helixi163 – 172Combined sources10
    Beta strandi176 – 181Combined sources6
    Beta strandi185 – 187Combined sources3
    Beta strandi193 – 195Combined sources3
    Helixi200 – 205Combined sources6

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP0A8F0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni130 – 1385-phospho-alpha-D-ribose 1-diphosphate bindingBy similarity9
    Regioni198 – 200Uracil bindingBy similarity3

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2EHJX-ray2.80A/B/C/D2-208[»]
    ProteinModelPortaliP0A8F0.
    SMRiP0A8F0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry databases

    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: November 2, 2016
    This is version 91 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.