Q128E4 · ENO_POLSJ
- ProteinEnolase
- Geneeno
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids427 (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 = H2O + phosphoenolpyruvate
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 | 163 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 205 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 242 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 285 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 312 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 337 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 337 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 366 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 367 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 388 | (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 > Betaproteobacteria > Burkholderiales > Comamonadaceae > Polaromonas
Accessions
- Primary accessionQ128E4
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_0000267071 | 1-427 | Enolase | |||
Sequence: MSAIVDIVGREILDSRGNPTVECDVLLESGVMGRAAVPSGASTGSREAIELRDGDKSRYLGKGVLKAVEHINTEISEAVLGLDASEQAFLDRTLIDLDGTDNKSRLGANATLAVSMAVARAAAEEAGLPLYRYFGGSGAMQMPVPMMNVVNGGAHANNNLDLQELMIIPIGAPSFREAVRYGAEVFHALKKILHDKGMSVAVGDEGGFAPNVPSHEAAIQMILEAIDKAGYVAGEQIALGLDCAASEFYKDGKYVLAGEGLSLDATEWTNILATWVDKYPIISIEDGMAEGDWDGWKILTERLGKQVQLVGDDLFVTNTKILKEGIDKHIANSILIKINQIGTLTETFAAIEMAKRAGYTAVISHRSGETEDSTIADIAVGTNAGQIKTGSLSRSDRMAKYNQLLRIEEDLGDIATYPGRAAFYNLR |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length427
- Mass (Da)45,678
- Last updated2006-08-22 v1
- ChecksumC8BBCB883A426284
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000316 EMBL· GenBank· DDBJ | ABE45098.1 EMBL· GenBank· DDBJ | Genomic DNA |