A0A0N1GX53 · A0A0N1GX53_9EURO
- ProteinMethylthioribulose-1-phosphate dehydratase
- GeneMDE1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids240 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic activity
- 5-(methylsulfanyl)ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 100 | substrate | |||
Binding site | 117 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 119 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 146 | Proton donor/acceptor | |||
Binding site | 202 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | methylthioribulose 1-phosphate dehydratase activity | |
Molecular Function | zinc ion binding | |
Biological Process | L-methionine salvage from methylthioadenosine | |
Biological Process | L-methionine salvage from S-adenosylmethionine |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMethylthioribulose-1-phosphate dehydratase
- EC number
- Short namesMTRu-1-P dehydratase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Phialophora
Accessions
- Primary accessionA0A0N1GX53
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 24-229 | Class II aldolase/adducin N-terminal | |||
Sequence similarities
Belongs to the aldolase class II family. MtnB subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length240
- Mass (Da)26,817
- Last updated2015-12-09 v1
- Checksum2C66F554D730F5EF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LFJN01000054 EMBL· GenBank· DDBJ | KPI34626.1 EMBL· GenBank· DDBJ | Genomic DNA |