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Literature summary for 2.7.7.65 extracted from

  • Ryjenkov, D.A.; Tarutina, M.; Moskvin, O.V.; Gomelsky, M.
    Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain (2005), J. Bacteriol., 187, 1792-1798.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed as an amino-terminal MBP fusion in Escherichia coli Cereibacter sphaeroides
overexpressed as an amino-terminal MBP fusion in Escherichia coli Borreliella burgdorferi

Organism

Organism UniProt Comment Textmining
Borreliella burgdorferi
-
-
-
Cereibacter sphaeroides
-
-
-
Cereibacter sphaeroides RSP3513
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation is required for catalytic activity Borreliella burgdorferi

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Cereibacter sphaeroides
recombinant protein Borreliella burgdorferi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP
-
Cereibacter sphaeroides cyclic di-3',5'-guanylate + diphosphate
-
?
GTP
-
Borreliella burgdorferi cyclic di-3',5'-guanylate + diphosphate
-
?
GTP
-
Cereibacter sphaeroides RSP3513 cyclic di-3',5'-guanylate + diphosphate
-
?
additional information no substrate: ATP, ADP, AMP, GDP, GMP,CTP, TTP, c-di-GMP, cAMP, and cGMP Cereibacter sphaeroides ?
-
?
additional information no substrate: ATP, ADP, AMP, GDP, GMP,CTP, TTP, c-di-GMP, cAMP, and cGMP Cereibacter sphaeroides RSP3513 ?
-
?

Subunits

Subunits Comment Organism
More the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain Cereibacter sphaeroides
More the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain Borreliella burgdorferi

Synonyms

Synonyms Comment Organism
Rrp1
-
Borreliella burgdorferi