UniProtKB - Q26998 (UPP_TOXGO)
Protein
Uracil phosphoribosyltransferase
Gene
uprt
Organism
Toxoplasma gondii
Status
Functioni
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.1 Publication
Catalytic activityi
- EC:2.4.2.92 Publications
Cofactori
Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP.1 Publication
Activity regulationi
Allosterically activated by GTP. Binding of GTP leads to 5-time activation of the enzyme.1 Publication
Kineticsi
- KM=3.5 µM for uracil2 Publications
- KM=216 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the absence of GTP)2 Publications
- 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
: UMP biosynthesis via salvage pathway Pathwayi
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:
- Uracil phosphoribosyltransferase (uprt)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 59 | GTPCombined sources1 Publication | 1 | |
Binding sitei | 68 | GTPCombined sources1 Publication | 1 | |
Binding sitei | 112 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication | 1 | |
Binding sitei | 129 | GTPCombined sources2 Publications | 1 | |
Binding sitei | 137 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources2 Publications | 1 | |
Binding sitei | 158 | GTPCombined sources2 Publications | 1 | |
Binding sitei | 164 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources2 Publications | 1 | |
Binding sitei | 229 | Uracil; via amide nitrogenCombined sources1 Publication | 1 | |
Binding sitei | 235 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 102 – 105 | GTPCombined sources1 Publication | 4 |
GO - Molecular functioni
- GTP binding Source: UniProtKB-KW
- uracil phosphoribosyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- nucleoside metabolic process Source: InterPro
- UMP salvage Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Allosteric enzyme, Glycosyltransferase, Transferase |
Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.4.2.9, 6411 |
UniPathwayi | UPA00574;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 |
Organismi | Toxoplasma gondii |
Taxonomic identifieri | 5811 [NCBI] |
Taxonomic lineagei | Eukaryota › Sar › Alveolata › Apicomplexa › Conoidasida › Coccidia › Eucoccidiorida › Eimeriorina › Sarcocystidae › Toxoplasma |
Organism-specific databases
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 59 | K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication | 1 | |
Mutagenesisi | 68 | R → A: GTP-induced enzymatic activation is reduced 2-fold. 1 Publication | 1 | |
Mutagenesisi | 128 | C → V: No effect on activity. Far less oxidation sensitive than wild-type. 1 Publication | 1 | |
Mutagenesisi | 150 | K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication | 1 | |
Mutagenesisi | 235 | D → A or N: No enzymatic activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000120783 | 1 – 244 | Uracil phosphoribosyltransferaseAdd BLAST | 244 |
Interactioni
Subunit structurei
Monomer. Forms homodimers in presence of substrates and homotetramers in the presence of GTP.
2 PublicationsStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q26998 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q26998 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 164 – 172 | 5-phospho-alpha-D-ribose 1-diphosphate bindingCombined sources2 Publications | 9 | |
Regioni | 234 – 236 | Uracil bindingCombined sources1 Publication | 3 |
Sequence similaritiesi
Belongs to the UPRTase family.Curated
Phylogenomic databases
OMAi | TYATRMP |
Family and domain databases
CDDi | cd06223, PRTases_typeI, 1 hit |
Gene3Di | 3.40.50.2020, 1 hit |
InterProi | View protein in InterPro IPR000836, PRibTrfase_dom IPR029057, PRTase-like |
SUPFAMi | SSF53271, SSF53271, 1 hit |
i Sequence
Sequence statusi: Complete.
Q26998-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U10246 Genomic DNA Translation: AAB60213.1 |
Genome annotation databases
EnsemblProtistsi | TGME49_312480-t26_1; TGME49_312480-t26_1; TGME49_312480 |
Similar proteinsi
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 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 | [»] | |
SMRi | Q26998 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
EnsemblProtistsi | TGME49_312480-t26_1; TGME49_312480-t26_1; TGME49_312480 |
Organism-specific databases
Phylogenomic databases
OMAi | TYATRMP |
Enzyme and pathway databases
UniPathwayi | UPA00574;UER00636 |
BRENDAi | 2.4.2.9, 6411 |
Miscellaneous databases
EvolutionaryTracei | Q26998 |
Family and domain databases
CDDi | cd06223, PRTases_typeI, 1 hit |
Gene3Di | 3.40.50.2020, 1 hit |
InterProi | View protein in InterPro IPR000836, PRibTrfase_dom IPR029057, PRTase-like |
SUPFAMi | SSF53271, SSF53271, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | UPP_TOXGO | |
Accessioni | Q26998Primary (citable) accession number: Q26998 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | November 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 103 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families