Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Gundlach, J.; Mehne, F.M.; Herzberg, C.; Kampf, J.; Valerius, O.; Kaever, V.; Stuelke, J.
    An essential poison: synthesis and degradation of cyclic di-AMP in Bacillus subtilis (2015), J. Bacteriol., 197, 3265-3274.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.85 membrane
-
 Bacillus subtilis 16020
-

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.85 Bacillus subtilis Q45589
-
-
2.7.7.85 Bacillus subtilis 168 Q45589
-
-
3.1.4.59 Bacillus subtilis P37484
-
-
3.1.4.59 Bacillus subtilis P46344
-
-
3.1.4.59 Bacillus subtilis 168 P37484
-
-
3.1.4.59 Bacillus subtilis 168 P46344
-
-

Synonyms

EC Number Synonyms Comment Organism
3.1.4.59 gdpP
-
 Bacillus subtilis
3.1.4.59 PgpH
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
2.7.7.85 physiological function enzyme forms a complex with the regulatory protein CdaR and the glucosamine-6-phosphate mutase GlmM. cCaA, cdaR, and GlmM form a gene cluster that is conserved throughout the firmicutes. Data suggest that GlmM and GlmS are involved in the control of cyclic di-AMP synthesis. They convert glutamine and fructose-6-phosphate to glutamate and glucosamine-1-phosphate. Cyclic di-AMP synthesis is enhanced if the cells are grown in the presence of glutamate compared to that in glutamine-grown cells Bacillus subtilis
3.1.4.59 physiological function both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to this accumulation by inactivation of the diadenylate cyclase CdaA Bacillus subtilis
3.1.4.59 physiological function both phosphodiesterases, GdpP and PgpH, contribute to the degradation of cyclic di-AMP. Accumulation of cyclic di-AMP in a GdpP PgpH double mutant is toxic for the cells, and the cells respond to accumulation by inactivation of the diadenylate cyclase CdaA Bacillus subtilis