Metal-dependent phosphatase with probable damage-control functions (PubMed:27322068). Shows phosphatase activity against several substrates, including sugar phosphates and p-nitrophenyl phosphate(pNPP) (PubMed:27322068). Prefers sugar phosphate substrates, including the extremely potent glycating agents ribose-5-phosphate and erythrose-4-phosphate (PubMed:27322068). Phosphatase activity is strongly promoted by several divalent cations but is it suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases. Activity is strongly promoted by Co(2+), Ni(2+), Mg(2+), Cu(2+) and Mn(2+) (PubMed:27322068). Activity is inhibited by EDTA (PubMed:27322068). kcat is 1.68 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.94 sec(-1) with ribose 5-phosphate as substrate. kcat is 1.1 sec(-1) with 2-desoxyribose 5-phosphate as substrate. Multimer. Subfamily II proteins have an EGMGR motif about 50 residues from the C-terminus (Probable). This motif lies near the metal-binding residues in the putative substrate-binding cleft 2 (Probable). Subfamily II proteins occur only in eukaryotes, in two forms: as a stand-alone unit in plants, and as a C-terminal domain of pantothenate kinases in plants, animals, and chytrid fungi (Probable). Belongs to the damage-control phosphatase family. Phosphopantetheine phosphatase II subfamily.