Enolase-like, C-terminal domain superfamily
IPR036849
Definition
The C-terminal domain of the enolase adopts a TIM barrel fold that contains a metal binding site PMID:11748244. Proteins containing this domain also include D-glucarate dehydratase-like proteins and some uncharacterised proteins PMID:15581566. Enolase [ec:4.2.1.11], also known as 2-phosphoglycerate dehydratase or phosphopyruvate hydratase, is a highly conserved metalloenzyme that catalyses the reversible dehydration of 2-phospho-D-glycerate (2-PG) to phosphoenolpyruvate (PEP), a key step in the glycolytic pathway. The enzyme requires magnesium ions as cofactors, with one Mg 2+ ion bound constitutively and a second coordinated via the substrate during catalysis. Structurally, enolase consists of two distinct domains: a smaller N-terminal domain and a larger C-terminal TIM barrel domain that contains the active site. Catalysis proceeds through a general acid-base mechanism involving two key residues a proton donor (Glu209) and a proton acceptor (Lys342) along with several residues that coordinate the substrate and metal ions. Beyond its essential role in central carbon metabolism, bacterial enolase exhibits moonlighting functions: it serves as a component of the RNA degradosome involved in mRNA processing and degradation and is also found on the cell surface, where it may contribute to host-pathogen interactions. Members of this family are ubiquitous across all domains of life, reflecting the fundamental importance of glycolysis in cellular energy production.
5 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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