A0A7X3DJP2 · A0A7X3DJP2_9FIRM
- ProteinPseudouridine-5'-phosphate glycosidase
- GenepsuG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids309 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Catalytic activity
- D-ribose 5-phosphate + uracil = psi-UMP + H2O
Cofactor
Note: Binds 1 Mn2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 27 | Proton donor | |||
Binding site | 89 | substrate | |||
Binding site | 109 | substrate | |||
Binding site | 141 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 143-145 | substrate | |||
Active site | 162 | Nucleophile | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydrolase activity, acting on glycosyl bonds | |
Molecular Function | metal ion binding | |
Molecular Function | pseudouridylate synthase activity | |
Biological Process | nucleobase catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePseudouridine-5'-phosphate glycosidase
- EC number
- Short namesPsiMP glycosidase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Oscillibacter
Accessions
- Primary accessionA0A7X3DJP2
Proteomes
Interaction
Subunit
Homotrimer.
Structure
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)32,613
- Last updated2021-06-02 v1
- ChecksumAA4E61FDD91BB41D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SCPG01000001 EMBL· GenBank· DDBJ | MUU11751.1 EMBL· GenBank· DDBJ | Genomic DNA |