P55859 · PNPH_BOVIN

  • Protein
    Purine nucleoside phosphorylase
  • Gene
    PNP
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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
Molecular Functionguanosine phosphorylase activity
Molecular Functionpurine-nucleoside phosphorylase activity
Biological Processpurine ribonucleoside salvage

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
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P55859
  • Secondary accessions
    • Q3ZBH6
    • Q58DQ2

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00001845351-289Purine nucleoside phosphorylase
Modified residue251Phosphoserine

Keywords

Proteomic databases

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Chemistry

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)
    32,037
  • Last updated
    2008-02-05 v3
  • Checksum
    7ECF84CCA494DEED
MANGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYSEIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVRVFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGENPLRGPNEERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFETVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESQGKANHEEVLEAGKQAAQKLEQFVSLLMASIPVSGHTG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 1; AA sequence
Sequence conflict25in Ref. 2; AAX46392

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BT021545
EMBL· GenBank· DDBJ
AAX46392.1
EMBL· GenBank· DDBJ
mRNA
BC103291
EMBL· GenBank· DDBJ
AAI03292.2
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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