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Information on EC 2.7.7.85 - diadenylate cyclase and Organism(s) Thermotoga maritima and UniProt Accession Q9WY43

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.85 diadenylate cyclase
IUBMB Comments
Cyclic di-3',5'-adenylate is a bioactive molecule produced by some bacteria and archaea, which may function as a secondary signalling molecule . The intracellular bacterial pathogen Listeria monocytogenes secretes it into the host's cytosol, where it triggers a cytosolic pathway of innate immunity .
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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9WY43
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
diadenylate cyclase, dna integrity scanning protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA integrity scanning protein
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cyclic-di-AMP synthase
-
-
-
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dacA
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-
-
-
disA
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:ATP adenylyltransferase (cyclizing)
Cyclic di-3',5'-adenylate is a bioactive molecule produced by some bacteria and archaea, which may function as a secondary signalling molecule [1]. The intracellular bacterial pathogen Listeria monocytogenes secretes it into the host's cytosol, where it triggers a cytosolic pathway of innate immunity [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ATP
2 diphosphate + cyclic di-3',5'-adenylate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ATP
2 diphosphate + cyclic di-3',5'-adenylate
show the reaction diagram
specific recognition of adenine in the active site pocked. The enzyme signals DNA structures that interfere with chromosome segregation cyclic di-3',5'-adenylate. The enzyme activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-dATP
competitive inhibitor of the diadenylate cyclase domain, binds in the same position as ATP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
3'-dATP
Thermotoga maritima
pH 9.5, 60°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme signals DNA structures that interfere with chromosome segregation cyclic di-3',5'-adenylate. The enzyme activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
339000
gel filtration, mutant D75N
353500
analytical ultracentrifugation
370000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallisation of apoenzyme, apoenzyme + ATPgammaS, apoenzyme + cordycepin-triphosphate, determination of the crystal structure at 2.1 A
structure in the presence of 3'-dATP and Mn2+. The metal ion is octahedrally coordinated with all six coordination positions occupied by oxygen ligands. The three phosphate groups from 3'-dATP together with Asp75 from the adjacent subunit and two water molecules are all located between 2.0 and 2.5 A from the manganese. The pre-reaction state shows a highly coordinated arrangement of the two ATP (-analogues) in almost optimal distance for the nucleophilic attack of the 3'-OH on the alpha-phosphate of the neighbouring ATP. The rate-limiting step of cyclic di-AMP synthesis by DisA is not defined by the reaction itself, but rather by the accessibility of the active site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Witte, G.; Hartung, S.; Buettner, K.; Hopfner, K.P.
Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates
Mol. Cell
30
167-178
2008
Bacillus subtilis (P37573), Bacillus subtilis, Thermotoga maritima (Q9WY43)
Manually annotated by BRENDA team
Mueller, M.; Deimling, T.; Hopfner, K.P.; Witte, G.
Structural analysis of the diadenylate cyclase reaction of DNA-integrity scanning protein A (DisA) and its inhibition by 3-dATP
Biochem. J.
469
367-374
2015
Thermotoga maritima (Q9WY43), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WY43)
Manually annotated by BRENDA team