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Protein

Uracil phosphoribosyltransferase

Gene

uprt

Organism
Toxoplasma gondii
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.1 Publication

Catalytic activityi

UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate.2 Publications

Cofactori

Mg2+1 PublicationNote: 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
  1. Vmax=0.45 µmol/min/mg enzyme2 Publications

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 (uprt)
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 sitei59GTPCombined sources1 Publication1
Binding sitei68GTPCombined sources1 Publication1
Binding sitei1125-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication1
Binding sitei129GTPCombined sources2 Publications1
Binding sitei1375-phospho-alpha-D-ribose 1-diphosphateCombined sources2 Publications1
Binding sitei158GTPCombined sources2 Publications1
Binding sitei1645-phospho-alpha-D-ribose 1-diphosphateCombined sources2 Publications1
Binding sitei229Uracil; via amide nitrogenCombined sources1 Publication1
Binding sitei2355-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi102 – 105GTPCombined sources1 Publication4

GO - Molecular functioni

GO - Biological processi

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:2.4.2.92 Publications)
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)DescriptionActionsGraphical viewLength
Mutagenesisi59K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication1
Mutagenesisi68R → A: GTP-induced enzymatic activation is reduced 2-fold. 1 Publication1
Mutagenesisi128C → V: No effect on activity. Far less oxidation sensitive than wild-type. 1 Publication1
Mutagenesisi150K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication1
Mutagenesisi235D → A or N: No enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001207831 – 244Uracil phosphoribosyltransferaseAdd BLAST244

Proteomic databases

PRIDEiQ26998.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi5811.TGME49_112480.

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 16Combined sources3
Helixi22 – 32Combined sources11
Beta strandi36 – 38Combined sources3
Helixi43 – 53Combined sources11
Helixi59 – 78Combined sources20
Beta strandi83 – 89Combined sources7
Turni91 – 93Combined sources3
Beta strandi95 – 101Combined sources7
Beta strandi105 – 111Combined sources7
Turni112 – 114Combined sources3
Helixi115 – 124Combined sources10
Beta strandi130 – 137Combined sources8
Beta strandi139 – 141Combined sources3
Beta strandi144 – 150Combined sources7
Helixi155 – 157Combined sources3
Beta strandi158 – 163Combined sources6
Beta strandi165 – 169Combined sources5
Helixi171 – 183Combined sources13
Helixi187 – 189Combined sources3
Beta strandi190 – 197Combined sources8
Helixi199 – 208Combined sources10
Beta strandi212 – 219Combined sources8
Beta strandi221 – 223Combined sources3
Beta strandi229 – 231Combined sources3
Helixi236 – 241Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ26998.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni164 – 1725-phospho-alpha-D-ribose 1-diphosphate bindingCombined sources2 Publications9
Regioni234 – 236Uracil bindingCombined sources1 Publication3

Sequence similaritiesi

Belongs to the UPRTase family.Curated

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
OMAiRVITGWI.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
InterProiIPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF14681. UPRTase. 1 hit.
[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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5811.TGME49_112480.

Proteomic databases

PRIDEiQ26998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG4203. Eukaryota.
COG0035. LUCA.
OMAiRVITGWI.

Enzyme and pathway databases

UniPathwayiUPA00574; UER00636.
BRENDAi2.4.2.9. 6411.

Miscellaneous databases

EvolutionaryTraceiQ26998.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
InterProiIPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF14681. UPRTase. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 85 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

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.