A0A8K0JVS8 · A0A8K0JVS8_LADFU
- ProteinPurine nucleoside phosphorylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids521 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Purine nucleoside phosphorylase involved in purine salvage.
Miscellaneous
Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it lacks several conserved amino acids in the substrate binding pocket that confer specificity towards MTA.
Catalytic activity
- a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Pathway
Purine metabolism; purine nucleoside salvage.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 51-52 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: RH | ||||||
Binding site | 84-85 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: TA | ||||||
Binding site | 156 | substrate | ||||
Sequence: M | ||||||
Binding site | 157 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 193 | Important for substrate specificity | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | S-methyl-5-thioadenosine phosphorylase activity | |
Biological Process | L-methionine salvage from methylthioadenosine | |
Biological Process | purine ribonucleoside salvage |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePurine nucleoside phosphorylase
- EC number
- Short namesPNP
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Palaeoptera > Odonata > Epiprocta > Anisoptera > Libellulidae > Ladona
Accessions
- Primary accessionA0A8K0JVS8
Proteomes
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-107 | Nucleoside phosphorylase | ||||
Sequence: IGIIGGTGISHSRIFSTERYIELQTPFGDPSGKIAVGRLGNTRLFFIPRHGWKHTIPPSVINYRANIWALKALGCTHVIGTTASCSLNDNMKPGDLLMLSSFINR | ||||||
Domain | 122-215 | Nucleoside phosphorylase | ||||
Sequence: ICHQNGLVVVVEGPRFPTVAESELYHSWGVDVISMTTVPEVCLAKELTLLYCCIASVSDYCSWNFQRKSLTVESVVKNFQENGIKVTNLIRRTL | ||||||
Compositional bias | 471-492 | Polar residues | ||||
Sequence: PGNMNTGSSRSTLNSQIKGTPR | ||||||
Region | 471-521 | Disordered | ||||
Sequence: PGNMNTGSSRSTLNSQIKGTPRKTKSSESKHSIQLSNLKSKTQTLPTVPDT | ||||||
Compositional bias | 500-521 | Polar residues | ||||
Sequence: KHSIQLSNLKSKTQTLPTVPDT |
Sequence similarities
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length521
- Mass (Da)58,241
- Last updated2022-08-03 v1
- Checksum73E8F406EB80C76A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 471-492 | Polar residues | ||||
Sequence: PGNMNTGSSRSTLNSQIKGTPR | ||||||
Compositional bias | 500-521 | Polar residues | ||||
Sequence: KHSIQLSNLKSKTQTLPTVPDT |
Keywords
- Technical term