A0A1L9P9M6 · A0A1L9P9M6_ASPVE
- ProteinS-methyl-5'-thioadenosine phosphorylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids804 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.
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
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.
Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 515 | phosphate (UniProtKB | ChEBI) | |||
Binding site | 561-562 | phosphate (UniProtKB | ChEBI) | |||
Binding site | 594-595 | phosphate (UniProtKB | ChEBI) | |||
Site | 678 | Important for substrate specificity | |||
Binding site | 696 | substrate | |||
Binding site | 697 | phosphate (UniProtKB | ChEBI) | |||
Binding site | 720-722 | substrate | |||
Site | 733 | Important for substrate specificity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | NADP binding | |
Molecular Function | phosphogluconate dehydrogenase (decarboxylating) activity | |
Molecular Function | S-methyl-5-thioadenosine phosphorylase activity | |
Biological Process | D-gluconate catabolic process | |
Biological Process | L-methionine salvage from methylthioadenosine | |
Biological Process | pentose-phosphate shunt, oxidative branch | |
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 > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionA0A1L9P9M6
Proteomes
Organism-specific databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 197-536 | 6-phosphogluconate dehydrogenase C-terminal | |||
Sequence similarities
Belongs to the 6-phosphogluconate dehydrogenase family.
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length804
- Mass (Da)88,137
- Last updated2017-03-15 v1
- ChecksumFFFDD7BCEE6EE4FB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KV878126 EMBL· GenBank· DDBJ | OJI98185.1 EMBL· GenBank· DDBJ | Genomic DNA |