Enolase-like superfamily (IPR034390)

Short name: Enolase-like_superfamily

Overlapping homologous superfamilies

Family relationships


Members of the enolase-like superfamily are related by their ability to catalyze the abstraction of a proton alpha to a carboxylic acid to form an enolate anion intermediate. This conserved partial reaction is mediated by conserved residues in the active site, including three residues used to bind a divalent metal involved in stabilization of the common intermediate. Reactions catalyzed by enzymes in this superfamily include racemization, beta-elimination of OH- or NH3, and cycloisomerization. Enzymes in this superfamily have two structural domains, an N-terminal capping domain, and a C-terminal TIM beta/alpha-barrel domain, both of which are required for function. In general, the catalytic residues can be found at the ends of the beta strands in the C-terminal barrel domain, while the residues required for substrate specificity are contained in the N-terminal domain. Although the TIM beta/alpha-barrel fold is common to many other superfamilies, none of these superfamilies show a significant level of sequence or functional similarity to the enolase-like superfamily [PMID: 8987982].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0046872 metal ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.