A0A2N3B6Y2 · A0A2N3B6Y2_9PROT
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids428 (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 | 156 | substrate | |||
Binding site | 164 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 165 | substrate | |||
Active site | 206 | Proton donor | |||
Binding site | 243 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 286 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 286 | substrate | |||
Binding site | 313 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 313 | substrate | |||
Active site | 338 | Proton acceptor | |||
Binding site | 338 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 365-368 | substrate | |||
Binding site | 367 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 368 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 389 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 389 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria
Accessions
- Primary accessionA0A2N3B6Y2
Proteomes
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
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)45,157
- Last updated2018-04-25 v1
- MD5 ChecksumEF257AACFBD1F2467B53A8479721772D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PHDZ01000013 EMBL· GenBank· DDBJ | PKP67215.1 EMBL· GenBank· DDBJ | Genomic DNA |