The genomic context suggests a role in the biosynthesis of modified polysaccharides; this association with genes involved in carbohydrate metabolism is observed in several phylogenetically distinct taxa. Is not expected to have peptidase activity despite low similarity to aminopeptidases. Binds 1 zinc ion per subunit. Homotrimer. Contains an N-terminal region with low similarity to aminopeptidases, an insert domain, and a C-terminal permutated winged helix-turn-helix domain. Belongs to the UPF0770 family. Has distant sequence similarity to aminopeptidases that belong to the MEROPS peptidase family M28, but binds only one zinc ion, contrary to the metallopeptidases of the MEROPS family M28 that bind two catalytic zinc ions. Lacks the active site Asp and Glu residues that are conserved in family members with aminopeptidase activity.