3'5'-cyclic nucleotide phosphodiesterase, catalytic domain (IPR002073)

Short name: PDEase_catalytic_dom

Overlapping homologous superfamilies

Domain relationships

  • HD/PDEase domain (IPR003607)
    • 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain (IPR002073)


The cyclic nucleotide phosphodiesterases (PDE) comprise a group of enzymes that degrade the phosphodiester bond in the second messenger molecules cAMP and cGMP. They are divided into 11 families. They regulate the localisation, duration and amplitude of cyclic nucleotide signalling within subcellular domains. PDEs are therefore important for signal transduction.

All of these forms contain a catalytic domain of approximately 270 amino acids at the carboxyl terminus. Regulatory domains that vary widely among the PDEase subfamilies flank the catalytic core and include regions that autoinhibit the catalytic domains as well as targeting sequences that control subcellular localization [PMID: 15260978].

PDEase catalytic domains adopt a compact alpha-helical structure consisting of 16 alpha-helices that can be divided into three subdomains. The active site of PDEases is a deep pocket formed by the tree subdomains and can be divided into two major subpockets for binding of divalent metals and substrate/inhibitors, respectively. The active site of all PDEase domains contains two divalent metal ions: zinc and probably magnesium [PMID: 15260978, PMID: 10846163, PMID: 17305581].

GO terms

Biological Process

GO:0007165 signal transduction

Molecular Function

GO:0004114 3',5'-cyclic-nucleotide phosphodiesterase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles