IUBMB Enzyme Nomenclature

EC 3.1.4.59

Accepted name: cyclic-di-AMP phosphodiesterase

Reaction: cyclic di-3',5'-adenylate + H2O = 5'-O-phosphonoadenylyl-(3'→5')-adenosine

For diagram of reaction click here.

Glossary: cyclic di-3',5'-adenylate = cyclic bis(3'→5')diadenylate
5'-O-phosphonoadenylyl-(3'→5')-adenosine = pApA

Other name(s): gdpP (gene name)

Systematic name: cyclic bis(3'→5')diadenylate 3'-adenylylhydrolase

Comments: The enzyme, described from Gram-positive bacteria, degrades the second messenger cyclic di-3',5'-adenylate. It is a membrane-bound protein that contains a cytoplasmic facing Per-Arnt-Sim (PAS) domain, a modified GGDEF domain, and a DHH/DHHA1 domain, which confers the phosphodiesterase activity. Activity requires Mn2+ and is inhibited by pApA.

Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:

References:

1. Rao, F., See, R.Y., Zhang, D., Toh, D.C., Ji, Q. and Liang, Z.X. YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity. J. Biol. Chem 285 (2010) 473-482. [PMID: 19901023]

2. Corrigan, R.M., Abbott, J.C., Burhenne, H., Kaever, V. and Grundling, A. c-di-AMP is a new second messenger in Staphylococcus aureus with a role in controlling cell size and envelope stress. PLoS Pathog. 7 (2011) e1002217. [PMID: 21909268]

3. Griffiths, J.M. and O'Neill, A.J. Loss of function of the gdpP protein leads to joint β-lactam/glycopeptide tolerance in Staphylococcus aureus. Antimicrob. Agents Chemother. 56 (2012) 579-581. [PMID: 21986827]

4. Bowman, L., Zeden, M.S., Schuster, C.F., Kaever, V. and Grundling, A. New insights into the cyclic di-adenosine monophosphate (c-di-AMP) degradation pathway and the requirement of the cyclic dinucleotide for acid stress resistance in Staphylococcus aureus. J. Biol. Chem 291 (2016) 26970-26986. [PMID: 27834680]

[EC 3.1.4.59 created 2019]


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