| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.4.59 | D420A | mutant exhibits residual activity against c-di-AMP, c-di-GMP, bis-p-nitrophenol phosphate, and thymidine monophosphate p-nitrophenol ester | Bacillus subtilis |
| 3.1.4.59 | D420A/D499A | mutation totally abolishes the catalytic activity | Bacillus subtilis |
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.4.59 | guanosine pentaphosphate | ppGpp is a strong competitive inhibitor of the DHH/DHHA1 domain | Bacillus subtilis |
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.4.59 | 0.0013 | - |
cyclic di-3',5'-adenylate | pH 8.3, temperature not specified in the publication | Bacillus subtilis | |
| 3.1.4.59 | 0.349 | - |
cyclic di-3',5'-guanylate | pH 8.3, temperature not specified in the publication | Bacillus subtilis |
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.4.59 | Co2+ | about 65% of the activity with Mn2+ | Bacillus subtilis | |
| 3.1.4.59 | Mg2+ | about 15% of the activity with Mn2+ | Bacillus subtilis | |
| 3.1.4.59 | Mn2+ | enzyme is strictly dependent on divalent cation, best cofactor is Mn2+ | Bacillus subtilis | |
| 3.1.4.59 | Ni2+ | about 55% of the activity with Mn2+ | Bacillus subtilis |
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.4.59 | Bacillus subtilis | P37484 | protein is a DHHA1 domain protein, COG3387 family member | - |
| 3.1.4.59 | Bacillus subtilis 168 | P37484 | protein is a DHHA1 domain protein, COG3387 family member | - |
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.4.59 | cyclic di-3',5'-adenylate + H2O | - |
Bacillus subtilis | 5'-O-phosphonoadenylyl-(3'->5')-adenosine | - |
? | |
| 3.1.4.59 | cyclic di-3',5'-adenylate + H2O | - |
Bacillus subtilis 168 | 5'-O-phosphonoadenylyl-(3'->5')-adenosine | - |
? | |
| 3.1.4.59 | cyclic di-3',5'-guanylate + H2O | - |
Bacillus subtilis | 5'-phosphoguanylyl-(3'->5')guanosine | - |
? | |
| 3.1.4.59 | cyclic di-3',5'-guanylate + H2O | - |
Bacillus subtilis 168 | 5'-phosphoguanylyl-(3'->5')guanosine | - |
? |
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.4.59 | YybT | - |
Bacillus subtilis |
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.4.59 | 0.23 | - |
cyclic di-3',5'-guanylate | pH 8.3, temperature not specified in the publication | Bacillus subtilis | |
| 3.1.4.59 | 0.55 | - |
cyclic di-3',5'-adenylate | pH 8.3, temperature not specified in the publication | Bacillus subtilis |
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.4.59 | 0.0359 | - |
guanosine pentaphosphate | pH 8.3, temperature not specified in the publication | Bacillus subtilis |
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.4.59 | physiological function | the DHH/DHHA1 domain hydrolyzes c-di-AMP and c-di-GMP to generate the linear dinucleotides 5'-pApA and 5'-pGpG. The atypical GGDEF domain of YybT exhibits ATPase activity. YybT participates in DNA damage and acid resistance | Bacillus subtilis |