A1RXU2 · MTAP_THEPD
- ProteinS-methyl-5'-thioadenosine phosphorylase
- GenemtnP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids262 (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
- phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
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 | 12 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 54-55 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: RH | ||||||
Binding site | 87-88 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: SA | ||||||
Site | 167 | Important for substrate specificity | ||||
Sequence: S | ||||||
Binding site | 185 | substrate | ||||
Sequence: M | ||||||
Binding site | 186 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 209-211 | substrate | ||||
Sequence: DYD | ||||||
Site | 220 | Important for substrate specificity | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 lineageArchaea > Thermoproteota > Thermoprotei > Thermofilales > Thermofilaceae > Thermofilum
Accessions
- Primary accessionA1RXU2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000415110 | 1-262 | S-methyl-5'-thioadenosine phosphorylase | |||
Sequence: MEKVKIGIIGGSGLYSPDFLTNPKEEKIYTPYGPPSSHVVIGEIAGRKVAFIPRHGKRHEIPPHKVNYRANIYALKELGVERLISVSAVGSLREDYKPGDFVCTDQFIDMTKGRVYTFYDGPVVAHVSMADPFCPELRELCIRSARKLGITMHEKGTYICIEGPRFSTRAESRLWRQFGADIIGMTLVPEVNLAREARMCFLNIAMVTDYDVWAEKPVTAHEVARVMAENTEKVKRLLADLIPSIPEERKCQCARALDEALI |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length262
- Mass (Da)29,467
- Last updated2007-02-06 v1
- Checksum0805BD30C4FB86E6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000505 EMBL· GenBank· DDBJ | ABL78022.1 EMBL· GenBank· DDBJ | Genomic DNA |