Diadenylate cyclase
DNA binding protein
diadenylate cyclase | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() Diadenylate cyclase homooctamer, Thermotoga maritima | |||||||||
Identifiers | |||||||||
EC no. | 2.7.7.85 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
Diadenylate cyclase EC 2.7.7.85, DNA integrity scanning protein DisA is a DNA binding protein[1] participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. Catalytic activity
- 2 ATP 2 diphosphate + cyclic di-3',5'-adenylate.
This enzyme has diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. This rate-limiting step is the accessibility of the active site; mutating the possible exit tunnel (residues 128-130) increases product 2-fold despite Arg-130 being important for ATP-binding. Does not convert GTP to c-di-GMP.
References
- ^ Witte G, Hartung S, Büttner K, Hopfner KP (April 2008). "Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates". Molecular Cell. 30 (2): 167–78. doi:10.1016/j.molcel.2008.02.020. PMID 18439896.
- v
- t
- e
Transferases: phosphorus-containing groups (EC 2.7)
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor | |
---|---|
2.7.2: COOH acceptor | |
2.7.3: N acceptor | |
2.7.4: PO4 acceptor |
(P2O7)
(PO4-nucleoside)
Polymerase |
| ||||
---|---|---|---|---|---|
Phosphorolytic 3' to 5' exoribonuclease | |||||
Nucleotidyltransferase | |||||
Guanylyltransferase | |||||
Other |
Phosphatidyltransferases | |
---|---|
Glycosyl-1-phosphotransferase |
(PO4; protein acceptor)
2.7.10: protein-tyrosine |
|
---|---|
2.7.11: protein-serine/threonine |
|
2.7.12: protein-dual-specificity |
|
2.7.13: protein-histidine |