Phosphatase which shows a preference for 4'-phosphopantetheine and its oxidatively damaged forms (sulfonate or S-sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein. May play a role in the physiological regulation of CoA intracellular levels. (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate (R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-sulfopantetheine + phosphate Activity is strongly promoted by Co(2+), Ni(2+), Mg(2+) and Mn(2+). Activity is inhibited by EDTA. Homodimer. Interacts with PKM. By glucose. Subfamily II proteins have an EGMGR motif about 50 residues from the C-terminus (By similarity). This motif lies near the metal-binding residues in the putative substrate-binding cleft 2 (By similarity). 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 (By similarity). In the N-terminal section; belongs to the type II pantothenate kinase family. In the C-terminal section; belongs to the damage-control phosphatase family. Phosphopantetheine phosphatase (II) subfamily. Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity.