Dual specificity cAMP and cGMP phosphodiesterase with marked preference for cyclic AMP, which is activated by cAMP and cGMP. Likely functions as a cAMP-stimulated cAMP-phosphodiesterase which may play a role in regulating the cAMP relay response. 3',5'-cyclic AMP + H2O = AMP + H(+) 3',5'-cyclic GMP + H2O = GMP + H(+) Divalent metal cation. Can use Mn(2+) or, to a lower extent, Mg(2+) or Zn(2+). Half-maximal activation occurs between 10 and 100 uM of Mn(2+) whereas maximal activation occurs with 10 mM of Zn(2+) or Mg(2+). cAMP/cGMP selectivity of 9. Optimum pH is 7.0. Low expression during growth. Mainly expressed after 8-10 hours of starvation when cells are aggregating and in the multicellular stage. The beta lactamase-like domain catalyzes the hydrolysis of cGMP. Belongs to the metallo-beta-lactamase superfamily. cNMP phosphodiesterase family.