A0A7I8DI44 · A0A7I8DI44_9FIRM
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids431 (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 + phosphoenolpyruvateThis reaction proceeds in the forward direction.
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 | 157 | substrate | ||||
Sequence: H | ||||||
Binding site | 165 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 166 | substrate | ||||
Sequence: E | ||||||
Active site | 207 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 244 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 289 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 289 | substrate | ||||
Sequence: E | ||||||
Binding site | 316 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 316 | substrate | ||||
Sequence: D | ||||||
Active site | 341 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 341 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 368-371 | substrate | ||||
Sequence: SHRS | ||||||
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 | ||||||
Binding site | 392 | substrate | ||||
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
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Anaerocolumna
Accessions
- Primary accessionA0A7I8DI44
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
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-136 | Enolase N-terminal | ||||
Sequence: IEKVIGREIIDSRGNPTVEAEVILKDGTIGRGAAPSGASTGIFEALELRDEDKSRFGGKGVLKAVANINGPISEALTGLNAADIYGVDAAMIALDGTKDKSGLGANAILAVSIAAARAAATSLMIPLYKFL | ||||||
Domain | 141-429 | Enolase C-terminal TIM barrel | ||||
Sequence: GNKLPVPMMNILNGGAHAANTVDVQEFMIMPAGASSFKEGLRQCTEVFHALAKILKEKGLATSVGDEGGFAPDLASDEEAIQLILQAIEKAGYVPGKDFVLAMDAASSEWKGEKPGEYILPKAGTHFTSKELIAHWKGLTEKYPIVSIEDGLDEEDWEGWQLLTKELGDKIQLVGDDLFVTNTTRLKKGIELGCGNSILIKLNQIGSVSETLEAIKMAHKAGYTAISSHRSGETEDTTIADLAVALNTCQIKTGAPSRTERVAKYNQLLRIEEDLGASAQYPGFDAFNI |
Sequence similarities
Belongs to the enolase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)45,753
- Last updated2021-04-07 v1
- Checksum6B448AE9053B9E2A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP023368 EMBL· GenBank· DDBJ | BCJ98002.1 EMBL· GenBank· DDBJ | Genomic DNA |