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Q26998

- UPP_TOXGO

UniProt

Q26998 - UPP_TOXGO

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Protein

Uracil phosphoribosyltransferase

Gene

uprt

Organism
Toxoplasma gondii
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg(2+) 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
Complete GO annotation...

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 – 163Combined sources
Helixi22 – 3211Combined sources
Beta strandi36 – 383Combined sources
Helixi43 – 5311Combined sources
Helixi59 – 7820Combined sources
Beta strandi83 – 897Combined sources
Turni91 – 933Combined sources
Beta strandi95 – 1017Combined sources
Beta strandi105 – 1117Combined sources
Turni112 – 1143Combined sources
Helixi115 – 12410Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi144 – 1507Combined sources
Helixi155 – 1573Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi165 – 1695Combined sources
Helixi171 – 18313Combined sources
Helixi187 – 1893Combined sources
Beta strandi190 – 1978Combined sources
Helixi199 – 20810Combined sources
Beta strandi212 – 2198Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi229 – 2313Combined sources
Helixi236 – 2416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAQVPASGKL LVDPRYSTND QEESILQDII TRFPNVVLMK QTAQLRAMMT
60 70 80 90 100
IIRDKETPKE EFVFYADRLI RLLIEEALNE LPFEKKEVTT PLDVSYHGVS
110 120 130 140 150
FYSKICGVSI VRAGESMESG LRAVCRGCRI GKILIQRDET TAEPKLIYEK
160 170 180 190 200
LPADIRDRWV MLLDPMCATA GSVCKAIEVL LRLGVKEERI IFVNILAAPQ
210 220 230 240
GIERVFKEYP KVRMVTAAVD ICLNSRYYIV PGIGDFGDRY FGTM
Length:244
Mass (Da):27,646
Last modified:November 1, 1996 - v1
Checksum:i1810CC234B2CE60F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10246 Genomic DNA. Translation: AAB60213.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10246 Genomic DNA. Translation: AAB60213.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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: November 26, 2014
This is version 75 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