A0A150IUQ6 · A0A150IUQ6_9EURY
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids432 (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 = phosphoenolpyruvate + H2O
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 | 161 | substrate | ||||
Sequence: H | ||||||
Binding site | 169 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 170 | substrate | ||||
Sequence: E | ||||||
Active site | 213 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 248 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 291 | substrate | ||||
Sequence: E | ||||||
Binding site | 318 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 318 | substrate | ||||
Sequence: D | ||||||
Active site | 343 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 343 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 370-373 | substrate | ||||
Sequence: SHRS | ||||||
Binding site | 372 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 373 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 394 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 394 | 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 lineageArchaea > Euryarchaeota > Stenosarchaea group > Candidatus Methanofastidiosia > Candidatus Methanofastidiosales > Candidatus Methanofastidiosaceae > Candidatus Methanofastidiosum
Accessions
- Primary accessionA0A150IUQ6
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 | 12-140 | Enolase N-terminal | ||||
Sequence: IIDIKSREVLDSRGNPTIETEIITGGGYGSAIVPSGASTGKHEALELRDKNDRYGGKGVLNAVRNVNEKITPLLIGMDIRKQREIDRVMIEEDGTENKSNLGANAILSVSLAAARCAADTINVPLYQYL | ||||||
Domain | 145-431 | Enolase C-terminal TIM barrel | ||||
Sequence: TYVLPVPMMNVINGGEHAGNELDFQEFMIMPVGAKSFSEALRICAEVYHQMKKVISKKYGKSSTNVGDEGGYAPPMKEISEPLEVIMSTLEELSYKDIVKIALDTASSTFYDEKTGTYNAMGKKMSPGELIDLFADVSSKYPIISIEDPMAEDDFEGFVEITKKLGKKIQIVGDDLFVTNKNRLSNGIKKGACNSLLLKVNQIGSLTEAIDTASLAYRSGYSVVVSHRSGETEDTMIADLAVGISSGQIKTGAPSRSERCAKYNRLLRIEEYLGESAVYAGKNFRIP |
Sequence similarities
Belongs to the enolase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length432
- Mass (Da)47,170
- Last updated2016-06-08 v1
- Checksum878E6DE70816B676
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LNGD01000136 EMBL· GenBank· DDBJ | KYC48682.1 EMBL· GenBank· DDBJ | Genomic DNA |