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Q26998

- UPP_TOXGO

UniProt

Q26998 - UPP_TOXGO

Protein

Uracil phosphoribosyltransferase

Gene

uprt

Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

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

    Enzyme regulationi

    Allosterically activated by GTP. Binding of GTP leads to 5-time activation of the enzyme.1 Publication

    Kineticsi

    1. KM=3.5 µM for uracil2 Publications
    2. KM=216 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the absence of GTP)2 Publications
    3. KM=37.4 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of GTP)2 Publications

    Vmax=0.45 µmol/min/mg enzyme2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei59 – 591GTP
    Binding sitei68 – 681GTP
    Binding sitei112 – 11215-phospho-alpha-D-ribose 1-diphosphate
    Binding sitei129 – 1291GTP
    Binding sitei137 – 13715-phospho-alpha-D-ribose 1-diphosphate
    Binding sitei158 – 1581GTP
    Binding sitei164 – 16415-phospho-alpha-D-ribose 1-diphosphate
    Binding sitei229 – 2291Uracil; via amide nitrogen
    Binding sitei235 – 23515-phospho-alpha-D-ribose 1-diphosphate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi102 – 1054GTP

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. uracil phosphoribosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. UMP salvage Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.4.2.9. 6411.
    UniPathwayiUPA00574; UER00636.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uracil phosphoribosyltransferase (EC:2.4.2.9)
    Short name:
    UPRT
    Short name:
    UPRTase
    Alternative name(s):
    UMP pyrophosphorylase
    Gene namesi
    Name:uprt
    OrganismiToxoplasma gondii
    Taxonomic identifieri5811 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication
    Mutagenesisi68 – 681R → A: GTP-induced enzymatic activation is reduced 2-fold. 1 Publication
    Mutagenesisi128 – 1281C → V: No effect on activity. Far less oxidation sensitive than wild-type. 1 Publication
    Mutagenesisi150 – 1501K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication
    Mutagenesisi235 – 2351D → A or N: No enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 244244Uracil phosphoribosyltransferasePRO_0000120783Add
    BLAST

    Proteomic databases

    PRIDEiQ26998.

    Interactioni

    Subunit structurei

    Monomer. Forms homodimers in presence of substrates and homotetramers in the presence of GTP.2 Publications

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 163
    Helixi22 – 3211
    Beta strandi36 – 383
    Helixi43 – 5311
    Helixi59 – 7820
    Beta strandi83 – 897
    Turni91 – 933
    Beta strandi95 – 1017
    Beta strandi105 – 1117
    Turni112 – 1143
    Helixi115 – 12410
    Beta strandi130 – 1378
    Beta strandi139 – 1413
    Beta strandi144 – 1507
    Helixi155 – 1573
    Beta strandi158 – 1636
    Beta strandi165 – 1695
    Helixi171 – 18313
    Helixi187 – 1893
    Beta strandi190 – 1978
    Helixi199 – 20810
    Beta strandi212 – 2198
    Beta strandi221 – 2233
    Beta strandi229 – 2313
    Helixi236 – 2416

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BD3X-ray1.93A/B/C/D2-244[»]
    1BD4X-ray2.20A/B/C/D2-244[»]
    1JLRX-ray2.45A/B/C/D2-244[»]
    1JLSX-ray2.50A/B/C/D2-244[»]
    1UPFX-ray2.30A/B/C/D21-244[»]
    1UPUX-ray2.50A/B/C/D21-244[»]
    ProteinModelPortaliQ26998.
    SMRiQ26998. Positions 10-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ26998.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni169 – 17245-phospho-alpha-D-ribose 1-diphosphate binding
    Regioni234 – 2363Uracil binding

    Sequence similaritiesi

    Belongs to the UPRTase family.Curated

    Phylogenomic databases

    OMAiPKLFYEK.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    InterProiIPR029057. PRTase-like.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q26998-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQVPASGKL LVDPRYSTND QEESILQDII TRFPNVVLMK QTAQLRAMMT    50
    IIRDKETPKE EFVFYADRLI RLLIEEALNE LPFEKKEVTT PLDVSYHGVS 100
    FYSKICGVSI VRAGESMESG LRAVCRGCRI GKILIQRDET TAEPKLIYEK 150
    LPADIRDRWV MLLDPMCATA GSVCKAIEVL LRLGVKEERI IFVNILAAPQ 200
    GIERVFKEYP KVRMVTAAVD ICLNSRYYIV PGIGDFGDRY FGTM 244
    Length:244
    Mass (Da):27,646
    Last modified:November 1, 1996 - v1
    Checksum:i1810CC234B2CE60F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10246 Genomic DNA. Translation: AAB60213.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10246 Genomic DNA. Translation: AAB60213.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BD3 X-ray 1.93 A/B/C/D 2-244 [» ]
    1BD4 X-ray 2.20 A/B/C/D 2-244 [» ]
    1JLR X-ray 2.45 A/B/C/D 2-244 [» ]
    1JLS X-ray 2.50 A/B/C/D 2-244 [» ]
    1UPF X-ray 2.30 A/B/C/D 21-244 [» ]
    1UPU X-ray 2.50 A/B/C/D 21-244 [» ]
    ProteinModelPortali Q26998.
    SMRi Q26998. Positions 10-244.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00544. Fluorouracil.

    Proteomic databases

    PRIDEi Q26998.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OMAi PKLFYEK.

    Enzyme and pathway databases

    UniPathwayi UPA00574 ; UER00636 .
    BRENDAi 2.4.2.9. 6411.

    Miscellaneous databases

    EvolutionaryTracei Q26998.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    InterProi IPR029057. PRTase-like.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
      Carter D., Donald R.G.K., Roos D., Ullman B.
      Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: RH / EP.
    2. "Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding."
      Schumacher M.A., Carter D., Scott D.M., Roos D.S., Ullman B., Brennan R.G.
      EMBO J. 17:3219-3232(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF MUTANT VAL-128 APOENZYME AND IN COMPLEXES WITH SUBSTRATES AND 5-FLUOROURACIL, MUTAGENESIS OF CYS-128.
    3. "The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
      Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
      Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235.

    Entry informationi

    Entry nameiUPP_TOXGO
    AccessioniPrimary (citable) accession number: Q26998
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Direct protein sequencing

    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