P85973 · PNPH_RAT
- ProteinPurine nucleoside phosphorylase
- GenePnp
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids289 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP85973
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000349126 | 1-289 | Purine nucleoside phosphorylase | |||
Sequence: MENEFTYEDYQRTAEWLRSHTKHRPQVAVICGSGLGGLTAKLTQPQAFDYNEIPNFPQSTVQGHAGRLVFGFLNGRSCVMMQGRFHMYEGYSLSKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFCGQNPLRGPNDERFGVRFPAMSDAYDRDMRQKAFNAWKQMGEQRELQEGTYIMSAGPTFETVAESCLLRMLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVVMDYNNLEKASHQEVLEAGKAAAQKLEQFVSILMESIPPRERAN |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length289
- Mass (Da)32,302
- Last updated2008-09-02 v1
- Checksum004486E55848749B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5Y9C1 | A0A8I5Y9C1_RAT | Pnp | 269 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH474040 EMBL· GenBank· DDBJ | EDL88431.1 EMBL· GenBank· DDBJ | Genomic DNA |