A0A1F6YI57 · A0A1F6YI57_9BACT
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids423 (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 | 171 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Active site | 213 | Proton donor | |||
Binding site | 251 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 294 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 321 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 346 | Proton acceptor | |||
Binding site | 346 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 375 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
Binding site | 398 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | |||
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
- Taxonomic lineageBacteria > Candidatus Nomurabacteria
Accessions
- Primary accessionA0A1F6YI57
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
- Length423
- Mass (Da)45,956
- Last updated2017-02-15 v1
- MD5 Checksum857254BDEE2AB0F89FDA51472D0192C2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MFVW01000025 EMBL· GenBank· DDBJ | OGJ06078.1 EMBL· GenBank· DDBJ | Genomic DNA |