Catalyzes the hydrolysis of phosphorylated glyceryl acetates in which the presence of a phosphate group is required for the enzymatic hydrolysis. Hydrolyzes a dibutyl glycerol derivative suggesting it acts on phosphoglycerol substrates with a butyrate leaving group. Also active with aromatic acetates and propionates. No activity with various sugar phosphates, with various nitrophenylphosphate or nitrophenylphosphonate derivatives, or with phosphorylated or non-phosphorylated sugar lactones tested. Does not hydrolyze non-phosphorylated carboxyesters with long chain leaving groups (PubMed:30277746). No general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities detected when tested with the following non-specific substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate (PubMed:9548740). Binds 2 Zn(2+) ions per subunit. Activity is higher in the enzyme containing Mn(2+) than that containing Zn(2+). kcat is 2.5 sec(-1) with 2-naphthyl acetate as substrate. kcat is 27 sec(-1) with (2S)-1,2-diacetyl glycerol-3-phosphate as substrate. kcat is 28 sec(-1) with rac-(2R,2S)-1,2-diacetyl glycerol-3-phosphate as substrate. Monomer. Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family.