O69174 · ENO_STAAU
- ProteinEnolase
- Geneeno
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids434 (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) (PubMed:26627653).
It is essential for the degradation of carbohydrates via glycolysis
It is essential for the degradation of carbohydrates via glycolysis
'Moonlights' as a laminin receptor. Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination.
Catalytic activity
- (2R)-2-phosphoglycerate = phosphoenolpyruvate + H2OThis reaction proceeds in the forward direction.
Cofactor
Note: Binds a second Mg2+ ion via substrate during catalysis.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.37 mM | 2-phosphoglycerate by octamer |
kcat is 83 sec-1 for octamer.
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 | 41 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 165 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 207 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 244 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 318 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 343 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 343 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 343 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 372 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 372 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 373 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 373 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 394 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 394 | phosphoenolpyruvate (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
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionO69174
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 135 | No longer forms homooctamers. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 138 | No longer forms homooctamers. | ||||
Sequence: G → A | ||||||
Mutagenesis | 139 | Significantly impairs homooctamer formation, no enzymatic activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 140 | Significantly impairs homooctamer formation. | ||||
Sequence: N → A | ||||||
Mutagenesis | 355 | Significantly impairs homooctamer formation, no enzymatic activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 389 | Slightly decrease in homooctamer formation, octomeric form has about 50% activity, dimeric form has none. | ||||
Sequence: N → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000133970 | 1-434 | Enolase | |||
Sequence: MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSQRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTLTETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKYDGIKSFYNLDK |
Interaction
Subunit
Homodimer and homooctamer; the homodimer is inactive (PubMed:26627653).
Structure
Sequence
- Sequence statusComplete
- Length434
- Mass (Da)47,117
- Last updated1998-08-01 v1
- ChecksumC4A19BA3675429B3
Keywords
- Technical term