A0A0E0BJ42 · A0A0E0BJ42_9ORYZ
- ProteinProbable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids518 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
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.
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 114 | substrate 1; for methylthioribulose-1-phosphate dehydratase activity | |||
Binding site | 132 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 134 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 157 | Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity | |||
Binding site | 207 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 282 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 284 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 417-418 | substrate 2; for enolase-phosphatase activity | |||
Binding site | 451 | substrate 2; for enolase-phosphatase activity | |||
Binding site | 477 | Mg2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity | |
Molecular Function | 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity | |
Molecular Function | acireductone synthase activity | |
Molecular Function | magnesium ion binding | |
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 nameProbable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
Including 2 domains:
- Recommended nameMethylthioribulose-1-phosphate dehydratase
- EC number
- Short namesMTRu-1-P dehydratase
- Recommended nameEnolase-phosphatase E1
- EC number
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza
Accessions
- Primary accessionA0A0E0BJ42
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-242 | Methylthioribulose-1-phosphate dehydratase | |||
Domain | 31-234 | Class II aldolase/adducin N-terminal | |||
Region | 279-518 | Enolase-phosphatase E1 | |||
Sequence similarities
In the C-terminal section; belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
In the N-terminal section; belongs to the aldolase class II family. MtnB subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length518
- Mass (Da)56,911
- Last updated2015-05-27 v1
- MD5 Checksum5524A8F9955A1CFF439B8476E9A95720
Keywords
- Technical term