P85973 · PNPH_RAT

  • Protein
    Purine nucleoside phosphorylase
  • Gene
    Pnp
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Pathway

Purine metabolism; purine nucleoside salvage.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site33phosphate (UniProtKB | ChEBI)
Binding site64phosphate (UniProtKB | ChEBI)
Binding site84-86phosphate (UniProtKB | ChEBI)
Binding site88a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site116phosphate (UniProtKB | ChEBI)
Binding site201a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site219a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site220phosphate (UniProtKB | ChEBI)
Binding site243a purine D-ribonucleoside (UniProtKB | ChEBI)
Site243Important for substrate specificity
Binding site257a purine D-ribonucleoside (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular region
Molecular Functionguanosine phosphorylase activity
Molecular Functionidentical protein binding
Molecular Functionnucleoside binding
Molecular Functionphosphate ion binding
Molecular Functionpurine nucleobase binding
Molecular Functionpurine-nucleoside phosphorylase activity
Biological Processallantoin metabolic process
Biological ProcessdAMP catabolic process
Biological Processdeoxyadenosine catabolic process
Biological Processdeoxyinosine catabolic process
Biological Processimmune response
Biological ProcessIMP catabolic process
Biological Processinosine catabolic process
Biological Processnicotinamide riboside catabolic process
Biological Processnucleobase-containing compound metabolic process
Biological Processnucleotide biosynthetic process
Biological Processpositive regulation of alpha-beta T cell differentiation
Biological Processpositive regulation of interleukin-2 production
Biological Processpositive regulation of T cell proliferation
Biological Processpurine ribonucleoside salvage
Biological Processpurine-containing compound salvage
Biological Processresponse to xenobiotic stimulus
Biological Processurate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Purine nucleoside phosphorylase
  • EC number
  • Short names
    PNP
  • Alternative names
    • Inosine phosphorylase
    • Inosine-guanosine phosphorylase

Gene names

    • Name
      Pnp
    • Synonyms
      Np

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P85973
  • Secondary accessions
    • A6KEC5

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00003491261-289Purine nucleoside phosphorylase

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    289
  • Mass (Da)
    32,302
  • Last updated
    2008-09-02 v1
  • Checksum
    004486E55848749B
MENEFTYEDYQRTAEWLRSHTKHRPQVAVICGSGLGGLTAKLTQPQAFDYNEIPNFPQSTVQGHAGRLVFGFLNGRSCVMMQGRFHMYEGYSLSKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFCGQNPLRGPNDERFGVRFPAMSDAYDRDMRQKAFNAWKQMGEQRELQEGTYIMSAGPTFETVAESCLLRMLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVVMDYNNLEKASHQEVLEAGKAAAQKLEQFVSILMESIPPRERAN

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I5Y9C1A0A8I5Y9C1_RATPnp269

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH474040
EMBL· GenBank· DDBJ
EDL88431.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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