|PROSITE documentation PDOC00837 [for PROSITE entry PS01092]|
Adenylate cyclase (EC 184.108.40.206) is the enzyme responsible for the synthesis of cAMP from ATP. From sequence data, it has been proposed [1,2] that there are three different classes of adenylate cyclases. Class I cyclases are found in enterobacteria and related Gram-negative bacteria. They are proteins of about 850 residues that consist of two functional domains: a N-terminal catalytic domain and a C-terminal regulatory domain.
As signature patterns we selected two highly conserved regions, the first one is located in the catalytic domain and the second one in the regulatory domain. The second signature includes a conserved histidine which could be phosphorylated by a PTS system IIA enzyme, thus leading to the activation of the cyclase.Expert(s) to contact by email:
November 1997 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|Title||Phylogeny of adenylyl cyclases.|
|Source||Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).|
|2||Authors||Barzu O., Danchin A.|
|Title||Adenylyl cyclases: a heterogeneous class of ATP-utilizing enzymes.|
|Source||Prog. Nucleic Acid Res. Mol. Biol. 49:241-283(1994).|