Q8DTS9 · ENO_STRMU
- ProteinEnolase
- Geneeno
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids432 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis.
'Moonlights' as a plasminogen receptor. Binds plasminogen and human salivary mucin MG2 when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity that may help the dissemination through oral tissues and entrance into the blood stream.
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 | 289 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 316 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 341 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 341 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 370 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 371 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 392 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | peptidoglycan-based cell wall | |
Cellular Component | phosphopyruvate hydratase complex | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphopyruvate hydratase activity | |
Molecular Function | zymogen binding | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEnolase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ8DTS9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000133979 | 1-432 | Enolase | |||
Sequence: MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEALIGYDVRDQQAIDKAMIALDGTPNKGKLGANAILGVSIAVARAAADFLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIVPAGAPTFKEALRWGAEIFHALKKILKERGLETAVGDEGGFAPKFDGTEDAVETIIKAIETAGYKPGEEVFLGFDCASSEFYDNGVYDYTKFEGEKGAKRSAAEQIDYIEELVNKYPIITIEDAMDENDWDGWKALTARLGDRVQLVGDDFFVTNTDYLARGIKEGAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADISVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK |
Post-translational modification
Probably phosphorylated (PubMed:15501816).
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length432
- Mass (Da)46,858
- Last updated2003-03-01 v1
- ChecksumC568723A72919037
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014133 EMBL· GenBank· DDBJ | AAN58930.1 EMBL· GenBank· DDBJ | Genomic DNA |