This superfamily entry represents a sugar 2,3-dehydratase, EvaA, that belongs to the "Nudix" hydrolase family, members of which often function as "housekeeping" enzymes. EvaA is organised as a dimer, each subunit of the dimer folds into two domains, which are related by a 2-fold rotational axis and which arose via gene duplication. Two binding sites for the dTDP-sugar ligands, pockets A and B, have been identified in each subunit. Site-directed mutagenesis experiments and activity assays strongly suggest that pocket A represents the active site and pocket B is a vestige of the gene duplication event.

DOI:10.1021/bi400176n, PFAM:PF03559