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Literature summary extracted from

  • Commichau, F.M.; Heidemann, J.L.; Ficner, R.; Stuelke, J.
    Making and breaking of an essential poison the cyclases and phosphodiesterases that produce and degrade the essential second messenger cyclic di-AMP in bacteria (2019), J. Bacteriol., 201, e00462-18 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.85 Mg2+ required Bacillus subtilis
2.7.7.85 Mg2+ required Streptococcus pneumoniae
2.7.7.85 Mg2+ required Listeria monocytogenes EGD
2.7.7.85 Mg2+ required Staphylococcus aureus
2.7.7.85 Mg2+ required Mycoplasma pneumoniae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.85 2 ATP Bacillus subtilis
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Streptococcus pneumoniae
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Listeria monocytogenes EGD
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Staphylococcus aureus
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Mycoplasma pneumoniae
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Listeria monocytogenes EGD EGD-e
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Bacillus subtilis 168
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Mycoplasma pneumoniae M129
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Listeria monocytogenes EGD ATCC BAA-679
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP Mycoplasma pneumoniae ATCC 29342
-
 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.85 Bacillus subtilis A0A6M3Z9Z6
-
-
2.7.7.85 Bacillus subtilis O31854
-
-
2.7.7.85 Bacillus subtilis P37573
-
-
2.7.7.85 Bacillus subtilis 168 A0A6M3Z9Z6
-
-
2.7.7.85 Bacillus subtilis 168 O31854
-
-
2.7.7.85 Bacillus subtilis 168 P37573
-
-
2.7.7.85 Listeria monocytogenes EGD Q8Y5E4
-
-
2.7.7.85 Listeria monocytogenes EGD ATCC BAA-679 Q8Y5E4
-
-
2.7.7.85 Listeria monocytogenes EGD EGD-e Q8Y5E4
-
-
2.7.7.85 Mycoplasma pneumoniae P75528
-
-
2.7.7.85 Mycoplasma pneumoniae ATCC 29342 P75528
-
-
2.7.7.85 Mycoplasma pneumoniae M129 P75528
-
-
2.7.7.85 Staphylococcus aureus Q9RL70
-
-
2.7.7.85 Streptococcus pneumoniae A0A0B7L730
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.85 2 ATP
-
 Bacillus subtilis 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Streptococcus pneumoniae 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Listeria monocytogenes EGD 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Staphylococcus aureus 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Mycoplasma pneumoniae 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Listeria monocytogenes EGD EGD-e 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Bacillus subtilis 168 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Mycoplasma pneumoniae M129 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Listeria monocytogenes EGD ATCC BAA-679 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?
2.7.7.85 2 ATP
-
 Mycoplasma pneumoniae ATCC 29342 2 diphosphate + cyclic di-3',5'-adenylate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.85 CdaA
-
 Listeria monocytogenes EGD
2.7.7.85 CdaA
-
 Bacillus subtilis
2.7.7.85 CdaA
-
 Staphylococcus aureus
2.7.7.85 CdaS
-
 Bacillus subtilis
2.7.7.85 Cyclic di-AMP synthase
-
 Bacillus subtilis
2.7.7.85 Dac
-
 Streptococcus pneumoniae
2.7.7.85 Dac
-
 Listeria monocytogenes EGD
2.7.7.85 Dac
-
 Bacillus subtilis
2.7.7.85 Dac
-
 Staphylococcus aureus
2.7.7.85 Dac
-
 Mycoplasma pneumoniae
2.7.7.85 dacA
-
 Streptococcus pneumoniae
2.7.7.85 dacA
-
 Listeria monocytogenes EGD
2.7.7.85 dacA
-
 Bacillus subtilis
2.7.7.85 dacA
-
 Staphylococcus aureus
2.7.7.85 DacB
-
 Mycoplasma pneumoniae
2.7.7.85 disA
-
 Bacillus subtilis
2.7.7.85 DNA integrity scanning protein DisA
-
 Bacillus subtilis
2.7.7.85 ybbP
-
 Streptococcus pneumoniae

General Information

EC Number General Information Comment Organism
2.7.7.85 evolution most bacteria possess only one diadenylate cyclase, either CdaA or DisA. In contrast, the spore-forming Gram-positive model organism Bacillus subtilis has the three enzymes, DisA, CdaA, and CdaS. The presence of three diadenylate cyclases is limited to members of the spore-forming genus Bacillus Bacillus subtilis
2.7.7.85 malfunction none of the corresponding genes is essential, but a strain lacking both DisA and CdaA is not viable under standard laboratory conditions Bacillus subtilis
2.7.7.85 metabolism CdaS is unable to replace the other enzymes since it is expressed only late during sporulation in the forespore but not in growing cells Bacillus subtilis
2.7.7.85 additional information the DAC domain is essential for activity Bacillus subtilis
2.7.7.85 additional information the DAC domain is essential for activity Streptococcus pneumoniae
2.7.7.85 additional information the DAC domain is essential for activity Listeria monocytogenes EGD
2.7.7.85 additional information the DAC domain is essential for activity Staphylococcus aureus
2.7.7.85 additional information the DAC domain is essential for activity Mycoplasma pneumoniae
2.7.7.85 physiological function in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes Streptococcus pneumoniae
2.7.7.85 physiological function in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes Listeria monocytogenes EGD
2.7.7.85 physiological function in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes Staphylococcus aureus
2.7.7.85 physiological function in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes Mycoplasma pneumoniae
2.7.7.85 physiological function in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes. None of the corresponding genes is essential Bacillus subtilis
2.7.7.85 physiological function in the diadenylate cyclases, one type of catalytic domain, the diadenylate cyclase (DAC) domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes. None of the corresponding genes is essential. CdaS is unable to replace the other enzymes since it is expressed only late during sporulation in the forespore but not in growing cells Bacillus subtilis