Q703Y8 · Q703Y8_THETE
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids412 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis.
Catalytic activity
- (2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds a second Mg2+ ion via substrate during catalysis.
Note: Mg2+ is required for catalysis and for stabilizing the dimer.
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 147 | substrate | |||
Binding site | 156 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 157 | substrate | |||
Active site | 200 | Proton donor | |||
Binding site | 236 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 279 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 279 | substrate | |||
Binding site | 305 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 305 | substrate | |||
Active site | 330 | Proton acceptor | |||
Binding site | 330 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 357-360 | substrate | |||
Binding site | 359 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 360 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 381 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 381 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | extracellular region | |
Cellular Component | phosphopyruvate hydratase complex | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphopyruvate hydratase activity | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEnolase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Thermoproteus
Accessions
- Primary accessionQ703Y8
Subcellular Location
UniProt Annotation
GO Annotation
Note: Fractions of enolase are present in both the cytoplasm and on the cell surface.
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-126 | Enolase N-terminal | |||
Domain | 131-410 | Enolase C-terminal TIM barrel | |||
Sequence similarities
Belongs to the enolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length412
- Mass (Da)44,055
- Last updated2004-07-05 v1
- MD5 ChecksumAB2ED189B0AD0A8501B9A0EA5D94E30B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ621325 EMBL· GenBank· DDBJ | CAF18506.1 EMBL· GenBank· DDBJ | Genomic DNA |