A0A0W0D108 · A0A0W0D108_CANGB
- Proteinphosphopyruvate hydratase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids437 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- (2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O
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 | 160 | substrate | |||
Binding site | 169 | substrate | |||
Active site | 212 | Proton donor | |||
Binding site | 247 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 296 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 296 | substrate | |||
Binding site | 321 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 321 | substrate | |||
Active site | 346 | Proton acceptor | |||
Binding site | 373-376 | substrate | |||
Binding site | 397 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fungal-type vacuole | |
Cellular Component | mitochondrion | |
Cellular Component | phosphopyruvate hydratase complex | |
Molecular Function | magnesium ion binding | |
Molecular Function | melatonin binding | |
Molecular Function | phosphopyruvate hydratase activity | |
Biological Process | glycolytic process | |
Biological Process | regulation of vacuole fusion, non-autophagic |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namephosphopyruvate hydratase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Nakaseomyces
Accessions
- Primary accessionA0A0W0D108
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-134 | Enolase N-terminal | |||
Domain | 144-434 | Enolase C-terminal TIM barrel | |||
Sequence similarities
Belongs to the enolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)46,739
- Last updated2016-03-16 v1
- ChecksumD8DAE343A84EB6B1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LLZZ01000112 EMBL· GenBank· DDBJ | KTB05696.1 EMBL· GenBank· DDBJ | Genomic DNA |