A5EW24 · ENO_DICNV
- ProteinEnolase
- Geneeno
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids430 (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
Note: Binds a second Mg2+ ion via substrate during catalysis.
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 | 164 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 206 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 243 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 286 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 313 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 338 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 338 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 367 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 368 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 389 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K |
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 > Gammaproteobacteria > Cardiobacteriales > Cardiobacteriaceae > Dichelobacter
Accessions
- Primary accessionA5EW24
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
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000337615 | 1-430 | Enolase | |||
Sequence: MTITISRIHALEILDSRGNPTLQVGVTLSDGSFAQAGVPSGASTGSREALELRDGDAQRYLGKGVQKALANVKNHFAPALIGKPIYDLAALDRIMLAQDGTDFKTHLGANAILGVSLALARAKGASLKKPLYAVLCPQEEYTLPVPMMNIINGGEHADNSVDIQEFMIVPAGFDRFSEALRAGSEIFHTLKKVLKEQGLNTAVGDEGGFAPDLPSNEAAFAVIMQAIERAGYRAGEQIFLAMDAAASEFYREGRYHLASEQKAYTSAEFVDYLADLCRRYPIVSIEDGLHESDWDGWQLLTQSLGERVQLVGDDLFVTNSAILQEGIDKGVANAILIKPNQIGSLSETLQTIALADAAHYAAIISHRSGETEDTTIADIAVATTATQIKTGSLCRSDRVAKYNRLLTIEDELGTRARYAAKAAFLGKIKA |
Interaction
Subunit
Component of the RNA degradosome, a multiprotein complex involved in RNA processing and mRNA degradation.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length430
- Mass (Da)46,242
- Last updated2007-06-12 v1
- Checksum2B8107E5433F1E9C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000513 EMBL· GenBank· DDBJ | ABQ13410.1 EMBL· GenBank· DDBJ | Genomic DNA |