| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.7 Nucleotidyltransferases |
| ID: | 2.7.7.85 |
|---|---|
| Description: | Diadenylate cyclase. |
| Alternative Name: |
Cyclic-di-AMP synthase. |
| Cath: | 1.10.150.20; 1.10.287.770; 1.20.1260.110; 3.40.1700.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.7.7.85 |
| BRENDA Enzyme Link: | BRENDA 2.7.7.85 |
| KEGG Enzyme Link: | KEGG2.7.7.85 |
| BioCyc Enzyme Link: | BioCyc 2.7.7.85 |
| ExPASy Enzyme Link: | ExPASy2.7.7.85 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.7.85 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.7.85 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.7.85 |
| IntEnz Enzyme Link: | IntEnz 2.7.7.85 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.7.85 |
| RHEA:35655 | 2 ATP = c-di-AMP + 2 diphosphate |
| RULE(radius=1) | ([*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]).([*:9]-[OH;+0:10].[*:11]=[P;H0;+0:12](-[*:13])(-[*:14])-[O;H0;+0:15]-[*:16])>>([*:9]-[O;H0;+0:10]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:11]=[P;H0;+0:12](-[*:13])(-[*:14])-[O;H0;+0:8]-[*:7]).[*:1]-[OH;+0:2].[*:16]-[OH;+0:15] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| c-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response. | Woodward JJ, Iavarone AT, Portnoy DA | 2010 Jun 25 | 20508090 |
| Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. | Witte G, Hartung S, Büttner K, Hopfner KP | 2008 Apr 25 | 18439896 |