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EC Tree
The expected taxonomic range for this enzyme is: Vibrio cholerae O1
Synonyms
3'-5'-cyclic AMP GMP cyclase, di-nucleotide cyclase Vibrio, DncV,
VC0179 , VC0179-like protein,
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3'-5'-cyclic AMP GMP cyclase
di-nucleotide cyclase Vibrio
3'-5'-cyclic AMP GMP cyclase
-
3'-5'-cyclic AMP GMP cyclase
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di-nucleotide cyclase Vibrio
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di-nucleotide cyclase Vibrio
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DncV
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VC0179
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VC0179-like protein
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ATP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
GTP + ATP = 2 diphosphate + cyclic Gp(3'-5')A
GTP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
ATP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
(3)
ATP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
(3)
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ATP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
-
-
-
-
GTP + ATP = 2 diphosphate + cyclic Gp(3'-5')A
(2)
GTP + ATP = 2 diphosphate + cyclic Gp(3'-5')A
(2)
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GTP + ATP = 2 diphosphate + cyclic Gp(3'-5')A
-
-
-
-
GTP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
(1)
GTP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
(1)
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GTP + GTP = 2 diphosphate + cyclic Gp(3'-5')G
-
-
-
-
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NTP:NTP nucleotidyltransferase (3',5'-cyclizing)
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ATP + ATP
2 diphosphate + cyclic Ap(3'-5')A
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
additional information
?
-
ATP + ATP
2 diphosphate + cyclic Ap(3'-5')A
-
-
?
ATP + ATP
2 diphosphate + cyclic Ap(3'-5')A
-
-
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
-
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
-
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
a mixture of GTP and ATP triggers the synthesis of cGAMP as the dominant product, with little c-di-AMP and c-di-GMP generated
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
DncV preferentially synthesizes a hybrid c-AMP-GMP molecule from ATP and GTP
-
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
a mixture of GTP and ATP triggers the synthesis of cGAMP as the dominant product, with little c-di-AMP and c-di-GMP generated
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
DncV preferentially synthesizes a hybrid c-AMP-GMP molecule from ATP and GTP
-
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
-
?
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
-
-
?
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
-
in presence of a mixture of GTP and ATP cGAMP is the dominant product, with little cyclic di-AMP and cyclic di-GMP generated
?
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
-
in presence of a mixture of GTP and ATP cGAMP is the dominant product, with little cyclic di-AMP and cyclic di-GMP generated
?
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
-
-
?
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
-
-
?
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
-
-
?
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
-
-
?
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
-
-
?
additional information
?
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in cytosolic samples from a Vibrio cholerae DncV deletion strain expressing wild-type DncV, only product cyclic Ap(3'-5')G is found, not cyclic Gp(3'-5')G or cyclic Ap(3'-5')A
-
?
additional information
?
-
DncV preferably recognizes ATP and GTP as acceptor and donor nucleotides, respectively, in the first nucleotidyl transfer reaction
-
?
additional information
?
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DncV preferably recognizes ATP and GTP as acceptor and donor nucleotides, respectively, in the first nucleotidyl transfer reaction
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?
additional information
?
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no activity with TTP, UTP and CTP
-
?
additional information
?
-
DncV preferably recognizes ATP and GTP as acceptor and donor nucleotides, respectively, in the first nucleotidyl transfer reaction
-
?
additional information
?
-
DncV preferably recognizes ATP and GTP as acceptor and donor nucleotides, respectively, in the first nucleotidyl transfer reaction
-
?
additional information
?
-
in cytosolic samples from a Vibrio cholerae DncV deletion strain expressing wild-type DncV, only product cyclic Ap(3'-5')G is found, not cyclic Gp(3'-5')G or cyclic Ap(3'-5')A
-
?
additional information
?
-
no activity with TTP, UTP and CTP
-
?
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ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
additional information
?
-
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
-
-
?
ATP + GTP
2 diphosphate + cyclic Ap(3'-5')G
-
-
-
?
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
-
in presence of a mixture of GTP and ATP cGAMP is the dominant product, with little cyclic di-AMP and cyclic di-GMP generated
-
?
GTP + ATP
2 diphosphate + cyclic Gp(3'-5')A
-
in presence of a mixture of GTP and ATP cGAMP is the dominant product, with little cyclic di-AMP and cyclic di-GMP generated
-
?
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
-
-
-
?
GTP + GTP
2 diphosphate + cyclic Gp(3'-5')G
-
-
-
?
additional information
?
-
in cytosolic samples from a Vibrio cholerae DncV deletion strain expressing wild-type DncV, only product cyclic Ap(3'-5')G is found, not cyclic Gp(3'-5')G or cyclic Ap(3'-5')A
-
-
?
additional information
?
-
in cytosolic samples from a Vibrio cholerae DncV deletion strain expressing wild-type DncV, only product cyclic Ap(3'-5')G is found, not cyclic Gp(3'-5')G or cyclic Ap(3'-5')A
-
-
?
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5-methyltetrahydrofolate di-glutamate
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5-methyltetrahydrofolic acid
-
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additional information
no activitation by binding to DNa required
-
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0.00169
5-methyltetrahydrofolate di-glutamate
Vibrio cholerae O1
25°C, pH not specified in the publication
0.0339
5-methyltetrahydrofolic acid
Vibrio cholerae O1
25°C, pH not specified in the publication
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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UniProt
brenda
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physiological function
disruption of the DncV gene causes a significant defect in intestinal colonization by Vibrio cholerae. Increased expression of DncV severely inhibits Vibrio cholerae chemotaxis, expression of DncV does not change overall motility
physiological function
-
disruption of the DncV gene causes a significant defect in intestinal colonization by Vibrio cholerae. Increased expression of DncV severely inhibits Vibrio cholerae chemotaxis, expression of DncV does not change overall motility
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DNCV_ECOLX
432
0
49276
Swiss-Prot
-
DNCV_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
436
0
49363
Swiss-Prot
-
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structure in complex with dGTP. DncV adopts an extended bilobed architecture characterized by a nucleotidyltransferase fold
structure of apo form and in complex with GTP and with dATP and dGTP, respectively. DncV adopts an extended bilobed architecture characterized by a nucleotidyltransferase fold. The ribose and triphosphate moieties of both GTP and ATP are bound to the donor and acceptor pockets in a similar manner. DncV efficiently catalyzes the phosphodiester linkage formation with ATP bound to the acceptor pocket, compared with GTP, thereby producing pppA(3'–5')pG preferentially
structures of wild-type and mutant D131A/D133A, both to 2.1 A resolution. Structure and topology are typical of the nucleotidyltransferase superfamily. The molecule has an elongated shape with a groove in the middle that separates the molecule into two distinct domains. The two catalytic aspartic acid residues (Asp131 and Asp133) are within a beta sheet that is located at the bottom wall of the substrate-binding groove of DncV. In complex with GTP, GTP1 is hydrogen bonded with one of the metal ions and the side chains of Ser114, Ser301, Lys287, Asp348, and Tyr117 at the inner wall of the groove. GTP2 is hydrogen bonded with the other bound metal ion and the side chains of Asp133, Asp193, and Asn112. Complex strucutures reveal 5-methyltetrahydrofolate diglutamate bound opposite the substrate-binding pocket
wild-type and mutant D131N/D133N. Catalytic residues are D131 and D133 in strand beta1, and D193 in strand beta5, and the G[G/S]xx motif is defined by residues G113-S114-F115-Q116 in a well-defined loop linking helix alpha5 and strand beta1
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D131N
mutation in conserved acidic residue, loss of activity
D131N/D133N
mutation in conserved acidic residues, loss of activity
D133N
mutation in conserved acidic residue, loss of activity
D193N
mutation in conserved acidic residue, loss of activity
D260A
residue involved in folate binding, protein cannort fold properly
F109P
residue involved in folate binding, enzyme activity is completely impaired
K287A
mutation in residue that participates in the interaction with diphosphate, impairs the ability to catalyze cyclic di-GMP formation
R108W
residue involved in folate binding, enzyme activity is completely impaired
R40A
residue involved in folate binding, enzyme activity is completely impaired
R44E
residue involved in folate binding, protein cannort fold properly
Y137R
residue involved in folate binding, enzyme activity is completely impaired
D131N
-
mutation in conserved acidic residue, loss of activity
D131N/D133N
-
mutation in conserved acidic residues, loss of activity
D133N
-
mutation in conserved acidic residue, loss of activity
D193N
-
mutation in conserved acidic residue, loss of activity
D260A
-
residue involved in folate binding, protein cannort fold properly
K287A
-
mutation in residue that participates in the interaction with diphosphate, impairs the ability to catalyze cyclic di-GMP formation
R108W
-
residue involved in folate binding, enzyme activity is completely impaired
R40A
-
residue involved in folate binding, enzyme activity is completely impaired
R44E
-
residue involved in folate binding, protein cannort fold properly
D131A/D133A
crystallization data
D131A/D133A
loss of catalytic activity
D131A/D133A
-
loss of catalytic activity
D131A/D133A
-
crystallization data
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expression in Escherichia coli
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Ming, Z.; Wang, W.; Xie, Y.; Ding, P.; Chen, Y.; Jin, D.; Sun, Y.; Xia, B.; Yan, L.; Lou, Z.
Crystal structure of the novel di-nucleotide cyclase from Vibrio cholerae (DncV) responsible for synthesizing a hybrid cyclic GMP-AMP
Cell Res.
24
1270-1273
2014
Vibrio cholerae O1 (Q9KVG7), Vibrio cholerae O1 ATCC 39315 (Q9KVG7)
brenda
Davies, B.W.; Bogard, R.W.; Young, T.S.; Mekalanos, J.J.
Coordinated regulation of accessory genetic elements produces cyclic di-nucleotides for V. cholerae virulence
Cell
149
358-370
2012
Vibrio cholerae O1 (Q9KVG7), Vibrio cholerae O1 ATCC 39315 (Q9KVG7)
brenda
Zhu, D.; Wang, L.; Shang, G.; Liu, X.; Zhu, J.; Lu, D.; Wang, L.; Kan, B.; Zhang, J.R.; Xiang, Y.
Structural biochemistry of a Vibrio cholerae dinucleotide cyclase reveals cyclase activity regulation by folates
Mol. Cell.
55
931-937
2014
Vibrio cholerae O1 (Q9KVG7), Vibrio cholerae O1 ATCC 39315 (Q9KVG7)
brenda
Kato, K.; Ishii, R.; Hirano, S.; Ishitani, R.; Nureki, O.
Structural basis for the catalytic mechanism of DncV, bacterial homolog of cyclic GMP-AMP synthase
Structure
23
843-850
2015
Vibrio cholerae O1 (Q6XGD8), Vibrio cholerae O1 (Q9KVG7), Vibrio cholerae O1 ATCC 39315 (Q6XGD8), Vibrio cholerae O1 ATCC 39315 (Q9KVG7)
brenda
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2.7.7.B24 3',5'-cyclic AMP-GMP cyclase
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