P55859 · PNPH_BOVIN
- ProteinPurine nucleoside phosphorylase
- GenePNP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids289 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the 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 (By similarity).
Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (By similarity).
Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (By similarity).
Catalytic activity
- inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine
Pathway
Purine metabolism; purine nucleoside salvage.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 33 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 64 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84-86 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: RFH | ||||||
Binding site | 88 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 116 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 201 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 219 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 220 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 243 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 243 | Important for substrate specificity | ||||
Sequence: N | ||||||
Binding site | 257 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | guanosine phosphorylase activity | |
Molecular Function | purine-nucleoside phosphorylase activity | |
Biological Process | purine ribonucleoside salvage |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePurine nucleoside phosphorylase
- EC number
- Short namesPNP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP55859
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000184535 | 1-289 | Purine nucleoside phosphorylase | |||
Sequence: MANGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESQGKANHEEVLEAGKQAAQKLEQFVSLLMASIPVSGHTG | ||||||
Modified residue | 251 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length289
- Mass (Da)32,037
- Last updated2008-02-05 v3
- Checksum7ECF84CCA494DEED
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 1; AA sequence | ||||
Sequence: A → Q | ||||||
Sequence conflict | 25 | in Ref. 2; AAX46392 | ||||
Sequence: P → S |
Keywords
- Technical term