Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q26998 (UPP_TOXGO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uracil phosphoribosyltransferase

Short name=UPRT
Short name=UPRTase
EC=2.4.2.9
Alternative name(s):
UMP pyrophosphorylase
Gene names
Name:uprt
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP. Ref.3

Enzyme regulation

Allosterically activated by GTP. Binding of GTP leads to 5-time activation of the enzyme. Ref.3

Pathway

Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.

Subunit structure

Monomer. Forms homodimers in presence of substrates and homotetramers in the presence of GTP. Ref.1 Ref.3

Sequence similarities

Belongs to the UPRTase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.5 µM for uracil Ref.1 Ref.3

KM=216 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the absence of GTP)

KM=37.4 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of GTP)

Vmax=0.45 µmol/min/mg enzyme

Ontologies

Keywords
   LigandGTP-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Allosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological_processUMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

uracil phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244Uracil phosphoribosyltransferase
PRO_0000120783

Regions

Nucleotide binding102 – 1054GTP
Region169 – 17245-phospho-alpha-D-ribose 1-diphosphate binding
Region234 – 2363Uracil binding

Sites

Binding site591GTP
Binding site681GTP
Binding site11215-phospho-alpha-D-ribose 1-diphosphate
Binding site1291GTP
Binding site13715-phospho-alpha-D-ribose 1-diphosphate
Binding site1581GTP
Binding site16415-phospho-alpha-D-ribose 1-diphosphate
Binding site2291Uracil; via amide nitrogen
Binding site23515-phospho-alpha-D-ribose 1-diphosphate

Experimental info

Mutagenesis591K → A: GTP-induced enzymatic activation is reduced 4-fold. Ref.3
Mutagenesis681R → A: GTP-induced enzymatic activation is reduced 2-fold. Ref.3
Mutagenesis1281C → V: No effect on activity. Far less oxidation sensitive than wild-type. Ref.2
Mutagenesis1501K → A: GTP-induced enzymatic activation is reduced 4-fold. Ref.3
Mutagenesis2351D → A or N: No enzymatic activity. Ref.3

Secondary structure

............................................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q26998 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1810CC234B2CE60F

FASTA24427,646
        10         20         30         40         50         60 
MAQVPASGKL LVDPRYSTND QEESILQDII TRFPNVVLMK QTAQLRAMMT IIRDKETPKE 

        70         80         90        100        110        120 
EFVFYADRLI RLLIEEALNE LPFEKKEVTT PLDVSYHGVS FYSKICGVSI VRAGESMESG 

       130        140        150        160        170        180 
LRAVCRGCRI GKILIQRDET TAEPKLIYEK LPADIRDRWV MLLDPMCATA GSVCKAIEVL 

       190        200        210        220        230        240 
LRLGVKEERI IFVNILAAPQ GIERVFKEYP KVRMVTAAVD ICLNSRYYIV PGIGDFGDRY 


FGTM 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10246 Genomic DNA. Translation: AAB60213.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ26998.
SMRQ26998. Positions 10-244.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00544. Fluorouracil.

Proteomic databases

PRIDEQ26998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAPKLFYEK.

Enzyme and pathway databases

BRENDA2.4.2.9. 6411.
UniPathwayUPA00574; UER00636.

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceQ26998.

Entry information

Entry nameUPP_TOXGO
AccessionPrimary (citable) accession number: Q26998
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways