M0FQI9 · M0FQI9_9EURY
- ProteinUracil phosphoribosyltransferase
- Geneupp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids226 (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 | 36-40 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KGLVK | ||||||
Binding site | 86 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 111 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 145-153 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: DPMLATGST | ||||||
Binding site | 211 | uracil (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 216-218 | uracil (UniProtKB | ChEBI) | ||||
Sequence: GDA | ||||||
Binding site | 217 | 5-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | GTP binding | |
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 lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionM0FQI9
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length226
- Mass (Da)24,502
- Last updated2013-04-03 v1
- ChecksumD235D0BB0635E4F2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOLE01000026 EMBL· GenBank· DDBJ | ELZ62321.1 EMBL· GenBank· DDBJ | Genomic DNA |