A0A3S7JA46 · A0A3S7JA46_9PROT
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids429 (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
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 | 155 | substrate | ||||
Sequence: H | ||||||
Binding site | 163 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 164 | substrate | ||||
Sequence: E | ||||||
Active site | 205 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 242 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 286 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 286 | substrate | ||||
Sequence: E | ||||||
Binding site | 313 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 313 | substrate | ||||
Sequence: D | ||||||
Active site | 338 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 338 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 365-368 | substrate | ||||
Sequence: SHRS | ||||||
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 | ||||||
Binding site | 389 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Candidatus Kinetoplastibacterium
Accessions
- Primary accessionA0A3S7JA46
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 | 4-134 | Enolase N-terminal | ||||
Sequence: IVDIIGREILDSRGQPTVECDVILESGIIGRASVPSGASTGSREALELRDEDSNRYLGKGVLKAVENINNEISESLIGLDSQNQKLIDNILIDLDGTENKERLGANAILATSMAVLKAAAQQSNLPLYRYL | ||||||
Domain | 139-426 | Enolase C-terminal TIM barrel | ||||
Sequence: PISMPVPMMNIINGGAHANNNLDIQEFMIIPVGAKSFREALRWGSEIFQILKKIIHNKGLSTAVGDEGGFAPNISNHDEAIKLIIKAIIDAGYEPGNQIFLGLDCACSELYHDGKYVLKSEGNLSLNSKDFVNILSNWCDQYPIITIEDGMSENDWDGWALLTEKLGSKIQLVGDDLFVTNSKILKEGINKKIANSILIKINQIGTITETFEAIDMAKRNGYSSIISHRSAETEDTTIADIAVGTNVMQIKTGSLSRSDRMAKYNQLLRIEEELTTSSIYAGYNAFSK |
Sequence similarities
Belongs to the enolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)46,862
- Last updated2019-05-08 v1
- ChecksumF0F979E9078E0109
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP025628 EMBL· GenBank· DDBJ | AWD32543.1 EMBL· GenBank· DDBJ | Genomic DNA |