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Literature summary for 3.1.4.60 extracted from

  • Bai, Y.; Yang, J.; Eisele, L.E.; Underwood, A.J.; Koestler, B.J.; Waters, C.M.; Metzger, D.W.; Bai, G.
    Two DHH subfamily 1 proteins in Streptococcus pneumoniae possess cyclic di-AMP phosphodiesterase activity and affect bacterial growth and virulence (2013), J. Bacteriol., 195, 5123-5132 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0239
-
5'-O-phosphonoadenylyl-(3'->5')-adenosine pH 7.5, 37°C Streptococcus pneumoniae D39

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane protein possesses two transmembrane helices Streptococcus pneumoniae D39 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Streptococcus pneumoniae D39

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae D39 A0A0H2ZNP2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-O-phosphonoadenylyl-(3'->5')-adenosine + H2O
-
Streptococcus pneumoniae D39 2 AMP
-
?
cyclic di-3',5'-adenylate + H2O
-
Streptococcus pneumoniae D39 5'-O-phosphonoadenylyl-(3'->5')-adenosine
-
?
additional information Pde2 directly hydrolyzes c-di-AMP into AMP. Additionally, Pde2 degrades 5'-O-phosphonoadenylyl-(3'->5')-adenosine into AMP. Pde2 prefers substrate 5'-O-phosphonoadenylyl-(3'->5')-adenosine Streptococcus pneumoniae D39 ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 35000, calculated from sequence Streptococcus pneumoniae D39
More protein possesses two transmembrane helices, a PAS domain, an atypical GGDEF domain, a DHH domain, and a DHHA1 domain Streptococcus pneumoniae D39

Synonyms

Synonyms Comment Organism
PDE2
-
Streptococcus pneumoniae D39
SPD_1153
-
Streptococcus pneumoniae D39

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Streptococcus pneumoniae D39

General Information

General Information Comment Organism
physiological function deletion of either isoform Pde1 or Pde2 results in a moderate increase of the c-di-AMP levels compared with the parental strain. Deletion of both genes results in an up to 4fold increase in c-di-AMP levels compared to that of the parental strain. Both Pde1 and Pde2 play a role in pneumococcal growth. Deletion of either isoform Pde1 or Pde2 reduces the growth rate slightly, and the double mutant synergizes the reduction Streptococcus pneumoniae D39