U2TJP8 · U2TJP8_STRPY
- ProteinPurine nucleoside phosphorylase DeoD-type
- GenedeoD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Catalytic activity
- a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + a purine nucleobase
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 4 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: H | ||||||
Binding site | 20 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 24 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 43 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 87-90 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: RVGT | ||||||
Binding site | 179-181 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: EME | ||||||
Binding site | 203-204 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: SD | ||||||
Active site | 204 | Proton donor | ||||
Sequence: D | ||||||
Site | 218 | Important for catalytic activity | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | purine-nucleoside phosphorylase activity | |
Molecular Function | uridine phosphorylase activity | |
Biological Process | nucleoside catabolic process | |
Biological Process | purine nucleoside metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePurine nucleoside phosphorylase DeoD-type
- EC number
- Short namesPNP
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionU2TJP8
Proteomes
Interaction
Subunit
Homohexamer; trimer of homodimers.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-222 | Nucleoside phosphorylase | ||||
Sequence: ILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKTLIRVGTAGAIDPEVHVRELVLAQAAATNSNIIRNDFPEFDFPQIADFGLLDKAYHIAREMGVTTHVGNVLSSDVFYTNMPERNMALGKLGVKAIEMEAAALYYLAAQHHVKALGIMTISDNLNDPTEDTTAEERQTTF |
Sequence similarities
Belongs to the PNP/UDP phosphorylase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length237
- Mass (Da)26,034
- Last updated2013-11-13 v1
- Checksum09667EF0A34732E8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AWPJ01000415 EMBL· GenBank· DDBJ | ERL06695.1 EMBL· GenBank· DDBJ | Genomic DNA |