F0V270 · F0V270_MYCS3
- ProteinEnolase
- Geneeno
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids540 (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
Note: Binds a second Mg2+ ion via substrate during catalysis.
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 | 179 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 221 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 261 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 315 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 342 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 367 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 367 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 396 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 397 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 418 | (2R)-2-phosphoglycerate (UniProtKB | ChEBI) | ||||
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 > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionF0V270
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, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-144 | Enolase N-terminal | ||||
Sequence: IENLFAYELIDSRGNPTVACIAKVAKGKFLSKKSFTAKVLVPSGASTGAKEALELRDGDSSRFGGKGVKKAVHYINYVLGPSLIENDVNPADQAELDRFLMDLDGTENKSRYGANTILAVSLSVAKAVAKAKGLPFYQYV | ||||||
Domain | 155-450 | Enolase C-terminal TIM barrel | ||||
Sequence: KYVLPLPMVNVINGGAHSDNSLDFQEFMFVPVGASSMHEAVRISAECFHALAKYLKSKGLSTAKGDEGGFAPNFNSNEEALNAMLIAIANAGYKAGVIHGHVAIALDCAASELYDSNTKLYKFKKMIKAGCLSEEAGTKGTVQMIDYYVDLVEKYPIISIEDPLAEDDYEGFALLQKRIGKKVQIVGDDLYCTNPELTQMGIEKGLSNSVLIKVNQIGTLSETLNTMSLAKKAGWSCIISHRSGETEDTTIADIAVGTAAGQIKTGSFSRSERIAKYNRLLEIEIDLTSVNSTFYG | ||||||
Region | 502-540 | Disordered | ||||
Sequence: VSAGVNPSEESEIKSMEAQKIEDDQEGEDKKKKSRFSKS | ||||||
Compositional bias | 514-540 | Basic and acidic residues | ||||
Sequence: IKSMEAQKIEDDQEGEDKKKKSRFSKS |
Sequence similarities
Belongs to the enolase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length540
- Mass (Da)58,736
- Last updated2011-05-03 v1
- Checksum243E731FF9CD2355
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 514-540 | Basic and acidic residues | ||||
Sequence: IKSMEAQKIEDDQEGEDKKKKSRFSKS |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FQ790233 EMBL· GenBank· DDBJ | CBZ40751.1 EMBL· GenBank· DDBJ | Genomic DNA |