J6EQW5 · J6EQW5_TRIAS
- ProteinS-methyl-5'-thioadenosine phosphorylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids275 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.
Catalytic activity
- S-methyl-5'-thioadenosine + phosphate = S-methyl-5-thio-alpha-D-ribose 1-phosphate + adenine
Pathway
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 7 | phosphate (UniProtKB | ChEBI) | |||
Binding site | 32-33 | phosphate (UniProtKB | ChEBI) | |||
Binding site | 65-66 | phosphate (UniProtKB | ChEBI) | |||
Site | 151 | Important for substrate specificity | |||
Binding site | 169 | substrate | |||
Binding site | 170 | phosphate (UniProtKB | ChEBI) | |||
Binding site | 193-195 | substrate | |||
Site | 206 | Important for substrate specificity | |||
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 nameS-methyl-5'-thioadenosine phosphorylase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Trichosporonales > Trichosporonaceae > Trichosporon
Accessions
- Primary accessionJ6EQW5
Proteomes
Organism-specific databases
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-228 | Nucleoside phosphorylase | |||
Sequence similarities
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)30,023
- Last updated2012-10-31 v1
- ChecksumD6EAE5E33810C5AE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ALBS01000336 EMBL· GenBank· DDBJ | EJT45082.1 EMBL· GenBank· DDBJ | Genomic DNA |