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Protein

Uracil phosphoribosyltransferase

Gene

upp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

    • GTP binding Source: UniProtKB-KW
    • identical protein binding Source: IntAct
    • uracil phosphoribosyltransferase activity Source: EcoCyc
    • uridine kinase activity Source: GO_Central

    GO - Biological processi

    Keywordsi

    Molecular functionAllosteric enzyme, Glycosyltransferase, Transferase
    LigandGTP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:URACIL-PRIBOSYLTRANS-MONOMER
    MetaCyc:URACIL-PRIBOSYLTRANS-MONOMER
    SABIO-RKiP0A8F0
    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: EcoCyc
    • membrane Source: UniProtKB

    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-2DPAGEiP0A8F0

    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, 30 interactors
    DIPiDIP-36228N
    IntActiP0A8F0, 6 interactors
    STRINGi316385.ECDH10B_2664

    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
    OMAiRICGYEI
    PhylomeDBiP0A8F0

    Family and domain databases

    CDDicd06223 PRTases_typeI, 1 hit
    HAMAPiMF_01218_B Upp_B, 1 hit
    InterProiView protein in InterPro
    IPR000836 PRibTrfase_dom
    IPR029057 PRTase-like
    IPR034332 Upp_B
    IPR005765 Ura_phspho_trans
    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
    PATRICifig|1411691.4.peg.4241

    Similar proteinsi

    Entry informationi

    Entry nameiUPP_ECOLI
    AccessioniPrimary (citable) accession number: P0A8F0
    Secondary accession number(s): P25532, P78095, Q8XAC7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: March 28, 2018
    This is version 101 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health