Esterase that catalyzes the deacetylation of acetyl-(R)-mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates. Binds 2 Zn(2+) ions per subunit. Homohexamer, dimer of trimers. Belongs to the metallo-dependent hydrolases superfamily. Atu3266/EF_0837 deacetylase family.