› › Function and Biology

Structure of PEP bound Enolase from Mycobacterium tuberculosis

Source organism: Mycobacterium tuberculosis
Biochemical function: metal ion binding
Biological process: glycolytic process
Cellular component: cell surface

Quick links

EC 4.2.1.11: Phosphopyruvate hydratase

Reaction catalysed:
2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
Systematic name:
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Alternative Name(s):
  • 14-3-2-protein
  • 2-phospho-D-glycerate hydro-lyase
  • 2-phosphoglycerate dehydratase
  • 2-phosphoglycerate enolase
  • 2-phosphoglyceric dehydratase
  • Enolase
  • Gamma-enolase
  • Nervous-system specific enolase
  • Phosphoenolpyruvate hydratase

GO terms

Sequence families

Pfam Protein families (Pfam)
PF00113
Domain description: Enolase, C-terminal TIM barrel domain
Occurring in:
  1. Enolase
The deposited structure of PDB entry 7e51 contains 8 copies of Pfam domain PF00113 (Enolase, C-terminal TIM barrel domain) in Enolase. Showing 1 copy in chain A.

PF03952
Domain description: Enolase, N-terminal domain
Occurring in:
  1. Enolase
The deposited structure of PDB entry 7e51 contains 8 copies of Pfam domain PF03952 (Enolase, N-terminal domain) in Enolase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR000941
Domain description: Enolase
Occurring in:
  1. Enolase
IPR020810
Domain description: Enolase, C-terminal TIM barrel domain
Occurring in:
  1. Enolase
IPR020809
Domain description: Enolase, conserved site
Occurring in:
  1. Enolase
IPR020811
Domain description: Enolase, N-terminal
Occurring in:
  1. Enolase

Quick links