Catalyzes the phosphorylation of pantothenate the first step in CoA biosynthesis. May play a role in the physiological regulation of the intracellular CoA concentration. Functionally redudant with PANK1 (PubMed:16897480). The phosphatase activity shows preference for normal or oxidatively damaged intermediates of 4'-phosphopantetheine, which provides strong indirect evidence that the phosphatase activity pre-empts damage in the CoA pathway (PubMed:27322068). Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms (PubMed:27322068). Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein (PubMed:27322068). (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) (R)-4'-phosphopantothenate + H2O = (R)-pantothenate + phosphate (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphate 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 phosphatases. Activity is strongly promoted by Co(2+), Ni(2+) and Mn(2+) (PubMed:27322068). Activity is inhibited by EDTA (PubMed:27322068). kcat is 1.99 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.26 sec(-1) with phosphopantetheine as substrate. kcat is 0.94 sec(-1) with 4'-phosphopantotheine-S-sulfonate as substrate. kcat is 0.52 sec(-1) with 4'-phosphopantothenate as substrate. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. A number of isoforms are produced. According to EST sequences. Highly expressed in leaves and developing seeds. Expressed in roots, stems and flowers. 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). No visible phenotype under normal growth conditions, but homozygous double mutants pank1-1 and pank2-1 are embryonic lethal. 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.