EC |
3.1.4.59 |
Accepted name: |
cyclic-di-AMP phosphodiesterase |
Reaction: |
cyclic di-3′,5′-adenylate + H2O = 5′-O-phosphonoadenylyl-(3′→5′)-adenosine |
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For diagram of cyclic di-3′,5′-adenylate biosynthesis and breakdown, 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, Gene, KEGG, MetaCyc, PDB |
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:e1002217 (2011). [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] |
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[EC 3.1.4.59 created 2019] |
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