A0AAD3S7A6 · A0AAD3S7A6_NEPGR
- ProteinProbable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids513 (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 | 102 | substrate 1; for methylthioribulose-1-phosphate dehydratase activity | ||||
Sequence: C | ||||||
Binding site | 120 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 122 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 145 | Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity | ||||
Sequence: E | ||||||
Binding site | 195 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 277 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 279 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 412-413 | substrate 2; for enolase-phosphatase activity | ||||
Sequence: SS | ||||||
Binding site | 446 | substrate 2; for enolase-phosphatase activity | ||||
Sequence: K | ||||||
Binding site | 472 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
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
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
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Nepenthaceae > Nepenthes
Accessions
- Primary accessionA0AAD3S7A6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-230 | Methylthioribulose-1-phosphate dehydratase | ||||
Sequence: MATTTQAYIESKPVQETKALITELCRQFYSQGWVGGTGGSITIKVHDDCIRKPQQLIIMSPSGVQKERMSPEDMYILSPDGTIISFPTPKPYPHKPPKCSDCAPIFMKAYQMRNAGAIIHSHGMESCLVTMINPGSKEFRITHMEMIKGIQGHGYYDELVVPIIENTAHERDLTNSLAGAIEAYPKSTAVLVRNHGIYVWGDSWISAKTQAECYHYLFDAAIKLYQLGLD | ||||||
Domain | 19-222 | Class II aldolase/adducin N-terminal | ||||
Sequence: ALITELCRQFYSQGWVGGTGGSITIKVHDDCIRKPQQLIIMSPSGVQKERMSPEDMYILSPDGTIISFPTPKPYPHKPPKCSDCAPIFMKAYQMRNAGAIIHSHGMESCLVTMINPGSKEFRITHMEMIKGIQGHGYYDELVVPIIENTAHERDLTNSLAGAIEAYPKSTAVLVRNHGIYVWGDSWISAKTQAECYHYLFDAAI | ||||||
Region | 274-513 | Enolase-phosphatase E1 | ||||
Sequence: IVLDIEGTATPISFVTDVLFPYACDNIGRHLRETYESAETRDDIELLRTQAQDDLEKGVAGAVPVPHLTERKEEVIAAVVANVEAMIKADRKITALKQLQGHIWRNGFQNKELEGVVFEDVPEALERWHASGIKVYIYSSGSRLAQRLLFGNTNFGDLRKYLSGYFDTTVGNKRESRSYMEIYESVGVDSPSELLFVTDVYEEAIAAKAAGLEVIISVRPGNGPLPKNHGFRMVNLFSEI |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)57,153
- Last updated2024-05-29 v1
- Checksum26860FF60D89F8F8
Keywords
- Technical term