This entry represents the C-terminal domain of the enolase, which 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].
Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH.
The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. J. Biol. Chem. 277 8306-11 2002
Gerlt JA, Babbitt PC, Rayment I.
Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch. Biochem. Biophys. 433 59-70 2005
Signatures from InterPro member databases are used to construct an entry.