A0A3G0ZFZ5 · A0A3G0ZFZ5_DUNSA
- ProteinProbable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids505 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 92 | substrate 1; for methylthioribulose-1-phosphate dehydratase activity | ||||
Sequence: C | ||||||
Binding site | 110 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 112 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 135 | Proton donor/acceptor; for methylthioribulose-1-phosphate dehydratase activity | ||||
Sequence: E | ||||||
Binding site | 185 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 270 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 272 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 400-401 | substrate 2; for enolase-phosphatase activity | ||||
Sequence: SS | ||||||
Binding site | 434 | substrate 2; for enolase-phosphatase activity | ||||
Sequence: K | ||||||
Binding site | 460 | 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
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
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Chlorophyta > core chlorophytes > Chlorophyceae > CS clade > Chlamydomonadales > Dunaliellaceae > Dunaliella
Accessions
- Primary accessionA0A3G0ZFZ5
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-220 | Methylthioribulose-1-phosphate dehydratase | ||||
Sequence: MEANEALPLAVVEAKALVCELCRLFYGQGWVSGTGGGISIKNHPDFIAMAPSGVQKERMQPEDIFVLDAKGQVVETPKAKPPPARPPKLSECSPLFMAAYELRNAGAVIHSHSLNALMATLLEPDSDEFSVTHLEMIKGIEGHGFYGHCVVPVIENTARECELTDRMRQAIAAYPQSNAVLVRRHGVYVWGKDWIQAKTQAESYEYLFQAAVEMRKLGMD | ||||||
Domain | 16-212 | Class II aldolase/adducin N-terminal | ||||
Sequence: ALVCELCRLFYGQGWVSGTGGGISIKNHPDFIAMAPSGVQKERMQPEDIFVLDAKGQVVETPKAKPPPARPPKLSECSPLFMAAYELRNAGAVIHSHSLNALMATLLEPDSDEFSVTHLEMIKGIEGHGFYGHCVVPVIENTARECELTDRMRQAIAAYPQSNAVLVRRHGVYVWGKDWIQAKTQAESYEYLFQAAV | ||||||
Region | 221-249 | Disordered | ||||
Sequence: AGRPPGPRSLPAAANSTVMNGTTEAPPSK | ||||||
Region | 267-505 | Enolase-phosphatase E1 | ||||
Sequence: IVLDIEGTVAPISFVADKLFPYARDNVKQHLEAHYGSEECQEDIQAIRQQAAQDASGPGIPDGTAGQAAVVDAVVAWVQAAIAADRKVTALKQLQGHIWRTGFEKGQLKAELFRDVPDALVEWRNAGLKTYIYSSGSREAQRQLFGHTQVGDMRPYLSGFFDTNSGPKTSPASYKDIALSIGADSPSQLLFATDVLAEAEAASAAGWQAVLVTRRGNKPIPAGHRFRVISSMGDLVKQL |
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
- Length505
- Mass (Da)54,666
- Last updated2019-02-13 v1
- ChecksumE1CE5AD7EF51F96A