A0A9W5T8I8 · A0A9W5T8I8_BABOV
- ProteinEnolase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids442 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvateThis reaction proceeds in the forward and the backward directions.
Cofactor
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 | 165 | substrate | ||||
Sequence: H | ||||||
Binding site | 174 | substrate | ||||
Sequence: E | ||||||
Active site | 217 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 252 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 300 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 300 | substrate | ||||
Sequence: E | ||||||
Binding site | 327 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 327 | substrate | ||||
Sequence: D | ||||||
Active site | 352 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 379-382 | substrate | ||||
Sequence: SHRS | ||||||
Binding site | 403 | substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoskeleton | |
Cellular Component | nucleus | |
Cellular Component | phosphopyruvate hydratase complex | |
Cellular Component | plasma membrane | |
Cellular Component | vacuole | |
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
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia
Accessions
- Primary accessionA0A9W5T8I8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-139 | Enolase N-terminal | ||||
Sequence: IKSVHAREILDSRGNPTVEVDLTTDTGVFRAACPSGASTGIYEALELRDGDKSRYLGKGVLKAVANVNTTIANGIKGHDATRQRCLDDLMVKNLDGSVNEWGHCKSKLGANAILVVSMAAARAAAAHKKQPLYQYL | ||||||
Domain | 149-440 | Enolase C-terminal TIM barrel | ||||
Sequence: KYVLPVPCLNVINGGSHAGNSLAMQEFMILPVGAPTFKEAIRMGCEVYHNLKKVINTKYGQDATNVGDEGGFAPNIKSAEEALDLLVESIKKAGFEGQVKIGMDVAASEFYVKESRSYNLGFKCESPNMKTAAEMVAYYKDLCNKYPIVSIEDPFDQDDWEAYKMLTAEIGAKVQIVGDDLLVTNPKRIQTALEKQACNALLLKVNQIGSVSEAIDACLLSHQNKWGVMVSHRSGETEDTFIADLVVALGTGQIKTGAPCRSERNAKYNQLIRIEEELGSRATYAGAAFRTC |
Sequence similarities
Belongs to the enolase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length442
- Mass (Da)47,869
- Last updated2023-11-08 v1
- Checksum4D0BA0187DC482F1
Keywords
- Technical term