Catalyzes the hydrolysis of the ester bond between the phosphatidic acid and alcohol moieties of phospholipids. Can catalyze a transphosphatidylation reaction in the presence of high concentrations of primary alcohols. Has also phosphatase activity toward p-nitrophenyl phosphate. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+) Binds 1 iron ion. Iron is essential for catalysis. Binds metal ions, iron, manganese or zinc. The ion could be involved in the binding of substrate and/or the release of the product. Activated by calcium. Allosterically activated by phosphatidic acid in the presence of calcium. Proteolytically cleaved PLD is more active than the full-length enzyme, but is no longer activated by phosphatidic acid. Optimum pH is 7.5-8.0. Full-length phospholipase D is a monomer in solution. Proteolytically cleaved PLD is a heterodimer composed of one phospholipase D catalytic chain and one phospholipase D regulatory chain. The N-terminal region contains the catalytic domain and the C-terminal region contains regulatory elements. In late stationary phase, is proteolytically cleaved to a more active form where the two parts of the molecule (phospholipase D catalytic chain and phospholipase D regulatory chain) are still tightly associated. Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. Belongs to the PhoD family.