A0A0D2FAN2 · A0A0D2FAN2_CLAB1
- ProteinS-methyl-5'-thioadenosine phosphorylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids660 (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 | 15 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 63-64 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: RH | ||||||
Binding site | 96-97 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: SA | ||||||
Site | 180 | Important for substrate specificity | ||||
Sequence: S | ||||||
Binding site | 198 | substrate | ||||
Sequence: M | ||||||
Binding site | 199 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 222-224 | substrate | ||||
Sequence: DYD | ||||||
Site | 235 | Important for substrate specificity | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | hydrolase activity | |
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 > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Cladophialophora
Accessions
- Primary accessionA0A0D2FAN2
Proteomes
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-257 | Nucleoside phosphorylase | ||||
Sequence: IAVIGGTGLEHLPDFRKAAILTVDTPWGPPSSPITILEHPSPTTGHPIPIAFLARHGPHHALAPHEVPSRANIAALRHIGVRCIIAFSAAGSLAEEVKPRDFVVPDQVIDRTKGVRPWTFFEEGVVCHVPFADPFDAKVGDVVRQCGHSLEGDGVVLHDSGTLIVMEGPQFSTRAESNLYRTWGGTVINMSTLPEAKLAAEAEIAYQVILMSTDYDCWHDVHGDVSVEMVMGHMRANAVNARRFIAAVL | ||||||
Domain | 339-581 | Phospholipase/carboxylesterase/thioesterase | ||||
Sequence: PGHSHTHTVIFLHGRDSSAHEFANELFDSEASPELADSDRTLPALLPTVRWVFPQAPMLWSARLRSEMPQWFDMWTTEDPREAEHAALQRPGLRRVVSQILHTLDSEERLVPTTRIFVCGISQGCAAAIAALISRDGNAWRRMAGLAGLAGLSSWMPRQVEVDEKEQGAHYHRPADCEAWRTLPVMLQHCADDEVITVSHGRHLRDELTNTWSHQGVEWSEYEDGRHWLNEPRGVDDLVGFLR |
Sequence similarities
Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length660
- Mass (Da)73,801
- Last updated2015-04-29 v1
- Checksum6AB8B3DA808EA7D7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KN846980 EMBL· GenBank· DDBJ | KIW99176.1 EMBL· GenBank· DDBJ | Genomic DNA |