Conserved Site

3'5'-cyclic nucleotide phosphodiesterase, conserved site (IPR023174)

Short name: PDEase_CS

Description

3'5'-cyclic nucleotide phosphodiesterases (EC:3.1.4.17) (PDEases) catalyze the hydrolysis of cAMP or cGMP to the corresponding nucleoside 5' monophosphates [PMID: 3025833]. There are at least seven different subfamilies of PDEases [PMID: 2159198]:

  • Type 1, calmodulin/calcium-dependent PDEases.
  • Type 2, cGMP-stimulated PDEases.
  • Type 3, cGMP-inhibited PDEases.
  • Type 4, cAMP-specific PDEases.
  • Type 5, cGMP-specific PDEases.
  • Type 6, rhodopsin-sensitive cGMP-specific PDEases.
  • Type 7, High affinity cAMP-specific PDEases.

All of these forms seem to share a conserved domain of about 270 residues. This entry has a signature pattern from a stretch of 12 residues that contains two conserved histidines.

The 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

No terms assigned in this category.

Molecular Function

GO:0008081 phosphoric diester hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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