P50389 · PNPH_SACS2
- ProteinPurine nucleoside phosphorylase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids236 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
154 μM | S-methyl-5'-thioadenosine | |||||
25.4 μM | adenosine | |||||
84 μM | inosine | |||||
113.6 μM | guanosine |
Temperature Dependence
Optimum temperature is 120 degrees Celsius. Highly thermostable.
Pathway
Purine metabolism; purine nucleoside salvage.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 5 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: H | ||||||
Binding site | 21 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 25 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 43 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 86-89 | phosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: RYGT | ||||||
Binding site | 163 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 180-182 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: EME | ||||||
Binding site | 204-205 | a purine D-ribonucleoside (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: SD |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | S-methyl-5-thioadenosine phosphorylase activity | |
Biological Process | nucleoside catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePurine nucleoside phosphorylase
- EC number
- Short namesPNP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Saccharolobus
Accessions
- Primary accessionP50389
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063195 | 1-236 | Purine nucleoside phosphorylase | |||
Sequence: MNPVHILAKKGEVAERVLVVGDPGRARLLSTLLQNPKLTNENRGFLVYTGKYNGETVSIATHGIGGPSIAIVLEELAMLGANVFIRYGTTGALVPYINLGEYIIVTGASYNQGGLFYQYLRDNACVASTPDFELTNKLVTSFSKRNLKYYVGNVFSSDAFYAEDEEFVKKWSSRGNIAVEMECATLFTLSKVKGWKSATVLVVSDNLAKGGIWITKEELEKSVMDGAKAVLDTLTS | ||||||
Disulfide bond | 125 | Interchain | ||||
Sequence: C |
Keywords
- PTM
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
Structure
Sequence
- Sequence statusComplete
- Length236
- Mass (Da)25,738
- Last updated1996-10-01 v1
- ChecksumF1570ECE8AA3D51B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z50181 EMBL· GenBank· DDBJ | CAA90560.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006641 EMBL· GenBank· DDBJ | AAK42818.1 EMBL· GenBank· DDBJ | Genomic DNA |