| General Information |
| MoonProt ID | 41 |
| First appeared in release | 1.0 |
| Name(s) | Enolase
|
| UniProt ID | Q9NDG0 (Q9NDG0_TRIVA), Unreviewed |
| GO terms | GO:0006096 glycolysis
GO:0000287 magnesium ion binding
GO:0004634 phosphopyruvate hydratase activity
GO:0016829 lyase activity
GO:0000015 phosphopyruvate hydratase complex |
| Organisms for which functions have been demonstrated | Trichomonas vaginalis |
| Sequence length | NA |
| FASTA sequence | NA |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-2,5 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Enolase, enzyme
2-phospho-D-glycerate => phosphoenolpyruvate + H2O
Carbohydrate degradation, glycolysis |
| References for function | |
| E.C. number | 4.2.1.11 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | plasminogen binding |
| References for function | Mundodi, V., Kucknoor, A. S. & Alderete, J. F. (2008). Immunogenic
and plasminogen-binding surface-associated a-enolase of Trichomonas
vaginalis.Infect Immun. 2008 Feb;76(2):523-31. Epub 2007 Dec 10.
PMID: 18070902 |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | cell surface |
| Comments | |