A0A1S2MGE2 · A0A1S2MGE2_9STAP
- ProteinUracil phosphoribosyltransferase
- Geneupp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids209 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic activity
- diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Cofactor
Note: Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP.
Activity regulation
Allosterically activated by GTP.
Pathway
Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 79 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 104 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 131-139 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: DPMLATGAS | ||||||
Binding site | 194 | uracil (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 199-201 | uracil (UniProtKB | ChEBI) | ||||
Sequence: GDA | ||||||
Binding site | 200 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | GTP binding | |
Molecular Function | guanine phosphoribosyltransferase activity | |
Molecular Function | hypoxanthine phosphoribosyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | uracil phosphoribosyltransferase activity | |
Biological Process | UMP salvage | |
Biological Process | uracil salvage |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUracil phosphoribosyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A1S2MGE2
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length209
- Mass (Da)23,215
- Last updated2017-04-12 v1
- ChecksumEB37C516AD5BD3D9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MODY01000005 EMBL· GenBank· DDBJ | OIJ29175.1 EMBL· GenBank· DDBJ | Genomic DNA |