P50389 · PNPH_SACS2

Function

function

Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA.

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
154 μMS-methyl-5'-thioadenosine
25.4 μMadenosine
84 μMinosine
113.6 μMguanosine

Temperature Dependence

Optimum temperature is 120 degrees Celsius. Highly thermostable.

Pathway

Purine metabolism; purine nucleoside salvage.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site5a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site21phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site25phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site43phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site86-89phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site163a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site180-182a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site204-205a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionS-methyl-5-thioadenosine phosphorylase activity
Biological Processnucleoside catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Purine nucleoside phosphorylase
  • EC number
  • Short names
    PNP
  • Alternative names
    • 5'-methylthioadenosine phosphorylase I
      (MTA phosphorylase I; MTAPI) (EC:2.4.2.28
      ) . EC:2.4.2.28 (UniProtKB | ENZYME | Rhea)

Gene names

    • Ordered locus names
      SSO2706

Organism names

Accessions

  • Primary accession
    P50389

Proteomes

Subcellular Location

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00000631951-236Purine nucleoside phosphorylase
Disulfide bond125Interchain

Keywords

Proteomic databases

Interaction

Subunit

Homohexamer; disulfide-linked. Trimer of homodimers, with three symmetric intersubunit disulfide bonds linking the dimers to one another.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    236
  • Mass (Da)
    25,738
  • Last updated
    1996-10-01 v1
  • Checksum
    F1570ECE8AA3D51B
MNPVHILAKKGEVAERVLVVGDPGRARLLSTLLQNPKLTNENRGFLVYTGKYNGETVSIATHGIGGPSIAIVLEELAMLGANVFIRYGTTGALVPYINLGEYIIVTGASYNQGGLFYQYLRDNACVASTPDFELTNKLVTSFSKRNLKYYVGNVFSSDAFYAEDEEFVKKWSSRGNIAVEMECATLFTLSKVKGWKSATVLVVSDNLAKGGIWITKEELEKSVMDGAKAVLDTLTS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z50181
EMBL· GenBank· DDBJ
CAA90560.1
EMBL· GenBank· DDBJ
Genomic DNA
AE006641
EMBL· GenBank· DDBJ
AAK42818.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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