A0A0V0PTR3 · A0A0V0PTR3_9RHOB
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids425 (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 | 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 | 285 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 285 | substrate | ||||
Sequence: E | ||||||
Binding site | 312 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 312 | substrate | ||||
Sequence: D | ||||||
Active site | 337 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 337 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 364-367 | substrate | ||||
Sequence: SHRS | ||||||
Binding site | 366 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 367 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 388 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 388 | 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 > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Paracoccus
Accessions
- Primary accessionA0A0V0PTR3
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
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-134 | Enolase N-terminal | ||||
Sequence: IIDIFAREILDSRGNPTVEVDVTLEDGTMGRAAVPSGASTGAHEAVEKRDGDKARYLGKGVLEAVAAVNGEIAENLIGEDATEQVAIDRMMIELDGTPNKGRLGANAILGVSLAVAKAAAEACSQPLYRYV | ||||||
Domain | 139-425 | Enolase C-terminal TIM barrel | ||||
Sequence: ARVLPVPMMNIINGGEHADNPIDIQEFMIMPVAAENIREAVRMGSEVFHTLKKELSSAGLATGVGDEGGFAPNLSSTRDALDFILKAIEKAGYQPGDDIMLALDCASTEYFKGGKYEMAGEGKSLSPAENVAYLEALCNDYPILSIEDGCAEDDWDGWKLLTDTLGGRVQLVGDDLFVTNPARLAEGIAKGCGNSLLVKVNQIGTLTETLDAVRMADRARYTSVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEMLGAAAEYAGKSILRG |
Sequence similarities
Belongs to the enolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length425
- Mass (Da)44,907
- Last updated2016-03-16 v1
- Checksum121FA2A953851D04