Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP (PubMed:16313172, PubMed:18757371). Can use 2',3'-cAMP, 2',3'-cGMP, 3',5'-cAMP, 3',5'-cGMP and 3',5'-cUMP (PubMed:16313172, PubMed:18757371, PubMed:19801656). Hydrolysis of 2',3'-cAMP produces a mixture of 3'-AMP (major product) and 2'-AMP (minor product) (PubMed:18757371). In vitro, is 150-fold more active in hydrolyzing 2',3'-cAMP than 3',5'-cAMP (PubMed:18757371). Can also hydrolyze the model substrates p-nitrophenyl phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)) and p-nitrophenyl phenylphosphonate (pNPPP) (PubMed:16313172, PubMed:18757371, PubMed:19801656). Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes (PubMed:16313172). May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall (PubMed:19801656). Overexpression elicits a transcriptional response that is independent of the phosphodiesterase activity. It does not alter the levels of cAMP-CRP regulated genes, even though cAMP levels are reduced in cells. a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-phosphate + H(+) 2',3'-cyclophospho-AMP + H2O = 3'-AMP + H(+) 2',3'-cyclophospho-AMP + H2O = adenosine 2'-phosphate + H(+) 2',3'-cyclophospho-GMP + H2O = 3'-GMP + H(+) a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+) 3',5'-cyclic AMP + H2O = AMP + H(+) 3',5'-cyclic GMP + H2O = GMP + H(+) Binds 1 Fe(3+) ion per subunit. Binds 1 Mn(2+) ion per subunit. Ca(2+) acts as an activator of the enzymatic activity and is able to promote the hydrolysis of substrates even in the absence of transition-metal ions, thus providing an effective strategy for the regulation of the enzymatic activity. Two Ca(2+) ions bind at a site different from the dinuclear transition-metal-ion binding site (PubMed:26662456). Activity is enhanced by magnesium or manganese. Activity decreases in the presence of orthovanadate and phosphotyrosine (PubMed:16313172). kcat is 2.8 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.55 sec(-1) with pNPP as substrate. kcat is 12.4 sec(-1) with bis(pNPP) as substrate. Optimum pH is 8.5-9.5. Homodimer. The C-terminal extension (CTE) is necessary for the localization to the cell wall and cell envelope (PubMed:19801656, PubMed:24970891). Phosphorylation at Thr-309 promotes cell wall localization (PubMed:26904001). The C-terminal extension (CTE) is used to better adjust the substrates into the active sites and mediates in vivo subcellular localization of the protein (PubMed:19801656, PubMed:24970891). It also modulates expression levels of Rv0805 in mycobacteria (PubMed:24970891). Phosphorylated on Thr-309 by the eukaryotic-type serine/threonine-protein kinases PknA, PknB and PknL. Phosphorylation does not affect the enzymatic activity, but it renders negative charge to the protein, promoting its localization on cell wall. Belongs to the cyclic nucleotide phosphodiesterase class-III family.