Metal-dependent phosphatase with probable damage-control functions (PubMed:27322068). Shows phosphatase activity against p-nitrophenyl phosphate (pNPP), but natural substrates have not been identified yet (PubMed:27322068). Low phosphatase activity against 8-oxo nucleotides suggests that it could hydrolyze oxidatively damaged purine nucleotides or their biosynthetic intermediates (PubMed:27322068). Phosphatase activity is strongly promoted by several divalent cation ions but is it suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatase activity (PubMed:27322068). The [2Fe-2S] cluster does not seem to be directly involved in catalysis (PubMed:27322068). Activity is strongly promoted by Co(2+), Ni(2+), Mg(2+), Mn(2+), Ca(2+), Zn(2+) and Cu(2+) (PubMed:27322068). Activity is inhibited by EDTA (PubMed:27322068). kcat is 1.00 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.20 sec(-1) with adenosine-5'-diphosphate as substrate. kcat is 0.12 sec(-1) with 8-oxo-2'-deoxyguanosine-5'-triphosphatee as substrate. Subfamily I proteins are distinguished by three conserved motifs: the CxxC motif localized near the N-terminus, the GNFE motif localized about 40 residues from the C-terminus, and the KC motif localized about 25 residues from the C-terminus (Probable). In the crystal structures of the subfamily I proteins, the side chains of the cysteines in the CxxC and KC motifs face each other across the rim of the putative substrate-binding cleft, and the GNFE motif lies deep in the cleft close to the metal-binding aspartate and asparagine (Probable). the 3 conserved cysteines in motifs CxxC and KC play a key role in the interaction with the Fe-containing chromophore, which is not directly involved in catalysis (Probable). Belongs to the damage-control phosphatase family. Nucleotides phosphatase I subfamily.