3.1.4.52: cyclic-guanylate-specific phosphodiesterase
This is an abbreviated version!
For detailed information about cyclic-guanylate-specific phosphodiesterase, go to the full flat file.
Reaction
Synonyms
Arr, BB0374, BCG_1419c, Bd1817, BifA, BinA, Blrp, BlrP1, blue light-regulated phophodiesterase, BpdA, BpdB, c-di-GMP phosphodiesterase, c-di-GMP-hydrolyzing-phosphodiesterase, c-di-GMP-specific PDE, c-di-GMP-specific phosphodiesterase, CC3396, CD0757, CdgC, CdpA, cyclic di-GMP phosphodiesterase, cyclic di-GMP-specific phosphodiesterase, cyclic nucleotide phosphodiesterase, cyclic-di-GMP phosphodiesterase, diguanylate cyclase/phosphodiesterase, Dos, EAL, EAL domain phosphodiesterase, FimX, GAF/HD-GYP protein, H-NOX-associated cyclic-di-GMP processing enzyme, HaCE, HD-GYP, HD-GYP domain cyclic di-GMP phosphodiesterases, HD-GYP domain cyclic dimeric GMP phosphodiesterase, HD-GYP domain cyclic-di-GMP phosphodiesterase, HD-GYP PDE, HD-GYP phosphodiesterase, MbaA, MtbDGC, MtbPDE, PA2567, PA3947, PA4108, PA4367, PA4781, PAS-GGDEF-EAL domain-containing protein, PDE, PDE-A, PdeA, PDEA1, PdeB, PdeC, PdeH, perma_0986, phosphodiesterase A, PmGH, Putative uncharacterized protein, RapA, RavR, RbdA, RocR, RpfG, RpfR, ScrG, SO0437, TM0186, TM_0186, VieA, YahA, YcgF, YfgF
ECTree
3.1.4.52 cyclic-guanylate-specific phosphodiesteraseAdvanced search results
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results (Engineering
Engineering on EC 3.1.4.52 - cyclic-guanylate-specific phosphodiesterase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E323Q
-
mutation in EAL motif, both catalytic activity and induction by GTP are not affected
L128C/G353C
-
the mutant shows higher catalytic efficiency at pH 7.5 and 20°C compared to the wild type enzyme under light and dark conditions
R93S
-
the mutant shows higher catalytic efficiency at pH 7.5 and 20°C compared to the wild type enzyme under light and dark conditions
S309C/S312C
-
inactive at pH 7.5 and 20°C under dark and light conditions
C406S
-
site-directed mutagenesis of enzyme MtbDGC, the mutant is catalytically inactive
D183A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
D222A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
D305A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
E185A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G284A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
H189A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
H221A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
H250A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
H276A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
H277A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
K225A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
K317A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
P286A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R314 A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Y285 A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
D305A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
G284A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
H189A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
-
H221A
-
site-directed mutagenesis, the mutant shows highly reduced catalytic activity compared to the wild-type enzyme
-
P286A
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
-
D295A
D296A
D318A
D347A
-
mutant is indistinguishable from enzyme null mutant. Loss of twitching activity and PO4 phage sensitivity, mutant fails to assemble surface pili
D56N
-
the RocR mutant exhibits a significantly smaller Km value than that of the wild type enzyme
E175A
E265A
E268A
E268Q
E352A
E352C
E352D
E352Q
E355A
E464A
-
the PA2567 mutant shows increased kcat and Km compared to the wild type enzyme
E475A
-
mutant is indistinguishable from enzyme null mutant. Loss of twitching activity and PO4 phage sensitivity, mutant fails to assemble surface pili
F297A
-
the RocR mutant shows decreased kcat and Km compared to the wild type RocR enzyme
F498A
-
the PA2567 mutation reduces the enzyme activity to below the measurable level
G346A
-
mutant is indistinguishable from enzyme null mutant. Loss of twitching activity and PO4 phage sensitivity, mutant fails to assemble surface pili
K316A
L477A
-
mutant is indistinguishable from enzyme null mutant. Loss of twitching activity and PO4 phage sensitivity, mutant fails to assemble surface pili
N233A
Q161A
Q372A
R179A
S302A
-
the RocR mutant shows decreased kcat and increased Km compared to the wild type RocR enzyme
S493A
-
the PA2567 mutation reduces the enzyme activity to below the measurable level
T267A
V476A
-
mutant is indistinguishable from enzyme null mutant. Loss of twitching activity and PO4 phage sensitivity, mutant fails to assemble surface pili
E634A
D289A
-
VCA0681, mutation in active site, eliminated VCA0681 repression of vpsL-lux, biofilm formation not repressed by mutant contrary to wild-type. Expression of the active-site mutant (D289A) in a luxO D47E strain has little effect on cyclic di-3',5'-guanylate levels
D289A
Vibrio cholerae serotype O1 El Tor C6706
-
VCA0681, mutation in active site, eliminated VCA0681 repression of vpsL-lux, biofilm formation not repressed by mutant contrary to wild-type. Expression of the active-site mutant (D289A) in a luxO D47E strain has little effect on cyclic di-3',5'-guanylate levels
-
DAA
additional information
D296A
site-directed mutagenesis, the mutant shows a 33.5fold reduced kcat and increased Km compared to the wild-type enzyme
D296A
-
the RocR mutant shows decreased kcat and increased Km compared to the wild type RocR enzyme
D318A
site-directed mutagenesis, the mutant shows a reduced kcat and altered Km compared to the wild-type enzyme
E268A
-
the RocR mutation reduces the enzyme activity to below the measurable level
E268Q
site-directed mutagenesis, the mutant shows a reduced kcat and altered Km compared to the wild-type enzyme
E352D
site-directed mutagenesis, the mutant shows a reduced kcat and altered Km compared to the wild-type enzyme
E352Q
site-directed mutagenesis, the mutant shows a reduced kcat and altered Km compared to the wild-type enzyme
E355A
site-directed mutagenesis, the mutant shows a 1.3fold reduced kcat and increased Km compared to the wild-type enzyme
Q161A
site-directed mutagenesis, the mutant shows increased Km compared to the wild-type enzyme
Q372A
site-directed mutagenesis, the mutant shows a reduced kcat and altered Km compared to the wild-type enzyme
R179A
site-directed mutagenesis, the mutant shows a 29.1fold reduced kcat and increased Km compared to the wild-type enzyme
T267A
site-directed mutagenesis, the mutant shows a reduced kcat and altered Km compared to the wild-type enzyme
DAA
EAL domain of ravR mutated (DAA): key residues E and L are substituted by D and A
DAA
-
EAL domain of ravR mutated (DAA): key residues E and L are substituted by D and A
-
additional information
-
disruption or deletion of binA increased biofilm formation in culture and leads to increased cellulose production. The phenotypes of the DELTAbinA mutant strain can be disrupted by insertions in genes in the bacterial cellulose biosynthesis cluster
additional information
-
construction of a pdeA pdeB double mutant and a pdeB single mutant. pdeB single mutant cells exhibit significantly increased flexing, indicating a role for cyclic di-GMP in motility. While virulence in needle-inoculated C3H/HeN mice does not appear to be altered significantly in pdeB mutant cells, these cells exhibit a reduced ability to survive in Ixodes scapularis ticks. All phenotypes are restored when the mutant is complemented
additional information
-
deletion of bpdA results in a dramatic decrease in flagellar promoter activities, and a flagellar mutant shows similar phenotypes to the bpdA and bpdB mutant strains in mouse models of infection. Genes bpdA and bpdB mutants exhibit decreased dissemination within immunocompetent mice. Flagellar transcription is strongly downregulated in the bpdA mutant
additional information
-
enzyme deletion mutant shows 80% reduction in catalytic activity. Isolated C-terminal EAL domain shows no significant reduxtion in catalytic activity
additional information
-
system development to survey the activity of putative c-di-GMP metabolic enzymes, method design and evaluation, overview. Generation of 19 inducible translational fusion constructs for genes encoding putative c-di-GMP phosphodiesterases from Clostridium difficile 630 in engineered Clostridium difficile strain NPS235. To construct a c-di-GMP-responsive biosensor, a chimeric ribo switch is engineered upstream of the coding sequence for green fluorescent protein with nucleotides -564 to-86 of Bacillus cereus gene bc_4140 of strain ATCC 14579, containing an M-box riboswitch promoter, aptamer, transcriptional terminator, and flanking sequences, as a scaffold, construction of c-di-GMP riboswitch reporter strains using main parts of the sequence from Bacillus cereus strain ATCC 14579, gene bc_4140, UniProt ID Q818V1 and the aptamer sequence from a c-di-GMP-responsive riboswitch (GEMM motif), of Bacillus cereus gene bce_0489, strain ATCC 10987
additional information
-
system development to survey the activity of putative c-di-GMP metabolic enzymes, method design and evaluation, overview. Generation of 19 inducible translational fusion constructs for genes encoding putative c-di-GMP phosphodiesterases from Clostridium difficile 630 in engineered Clostridium difficile strain NPS235. To construct a c-di-GMP-responsive biosensor, a chimeric ribo switch is engineered upstream of the coding sequence for green fluorescent protein with nucleotides -564 to-86 of Bacillus cereus gene bc_4140 of strain ATCC 14579, containing an M-box riboswitch promoter, aptamer, transcriptional terminator, and flanking sequences, as a scaffold, construction of c-di-GMP riboswitch reporter strains using main parts of the sequence from Bacillus cereus strain ATCC 14579, gene bc_4140, UniProt ID Q818V1 and the aptamer sequence from a c-di-GMP-responsive riboswitch (GEMM motif), of Bacillus cereus gene bce_0489, strain ATCC 10987
-
additional information
-
both full-length enzyme and the isolated EAL domain hydrolyze cyclic diguanylate. Hydrolysis of 5-phosphoguanylyl(3-5)guanosine to guanosine monophosphate by isolated domain EAL is very poor
additional information
-
enzyme disruption mutant renders the cells unable to divide properly. Enzyme gene is co-transcribed with cyclic guanylate cyclase YvvD
additional information
-
disruption in the yfgF gene by linear transformation, phenotype, overview. The mutant is more sensitive to stress than the parent strain
additional information
-
expression of Mtbdgc in Mycobacterium smegmatis complements the MSDGC-1 knock out strain by restoring the long term survival of Mycobacterium smegmatis
additional information
-
deletion of either the GGDEF or the EAL domain results in a phenotype indistinguishable from enzyme deletion mutant. Deletion of the amino-terminal REC domain containing a putative polar localization signal results in a protein that still supports intermediate levels of pilus assembly and function, but is no longer localized to the bacterial pole. Enzyme deletion mutant is as virulent as wild-type in a murine model of acute pneumonia
additional information
-
deletion of gene PA4367 results in severe defect in swarming motility and a hyperbiofilm phenotype. Mutant exhibits increased cellular pools of cyclic di-3,5-guanylate, increased synthesis of a polysaccharide produced by the pel locus and decreased flagellar reversals. GGDQF and EAL domains of BifA are both required for complementation of the mutant
additional information
-
mutation of Arr leads to suppression of induction of biofilm formation
additional information
-
deletion of the PAS domain or substitution of the key residues implicated in sensing low-oxygen stress abrogates the functionality of RbdA
additional information
construction of a truncated enzyme version PA4781HD-GYP lacking the REC domain, the recombinant mutant shows highly reduced activity compared to thw wild-type enzyme
additional information
construction of a truncated enzyme version PA4781HD-GYP lacking the REC domain, the recombinant mutant shows highly reduced activity compared to thw wild-type enzyme
additional information
-
construction of a truncated enzyme version PA4781HD-GYP lacking the REC domain, the recombinant mutant shows highly reduced activity compared to thw wild-type enzyme
additional information
generation of GFP-tagged or untagged markerless in-frame deletion mutants and chromosomal gene replacement
additional information
-
generation of GFP-tagged or untagged markerless in-frame deletion mutants and chromosomal gene replacement
additional information
Shewanella oneidensis MR-1 / ATCC 700550
-
generation of GFP-tagged or untagged markerless in-frame deletion mutants and chromosomal gene replacement
-
additional information
-
removal of the EAL domain reverses enzyme activity, converting it to an inhibitor of swarming and activator of cps gene expression
