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5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
additional information
?
-
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in the biosynthesis of thiamine diphosphate
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme uses an iron-sulfur cluster as well as a 5'-deoxyadenosyl radical as cofactors to rearrange the 5-amino-imidazole ribonucleotide (AIR) substrate to the pyrimidine ring
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in the biosynthesis of thiamine diphosphate
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
the enzyme is involved in thiamine biosynthesis
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
mechanistic analysis
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in the biosynthesis of thiamine diphosphate
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
optimal assay condition is set both by using flavodoxin, flavodoxin reductase, and NADPH to reduce the [4Fe-4S] cluster of ThiC and by obviation of the prolonged reaction time to minimize the uncoupled AdoH production
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
4-amino-2-methyl-5-phosphomethylpyrimidine is sequentially phosphorylated and combined with 4-methyl-5-(2-hydroxyethyl)-thiazole phosphate to generate thiamine monophosphate before a final phosphorylation generates the active cofactor thiamine diphosphate
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
the product 4-amino-2-methyl-5-phosphomethylpyrimidine is an intermediate of thiamine pdiphosphate (coenzyme B1) biosynthesis
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
optimal assay condition is set both by using flavodoxin, flavodoxin reductase, and NADPH to reduce the [4Fe-4S] cluster of ThiC and by obviation of the prolonged reaction time to minimize the uncoupled AdoH production
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
ThiC undergoes multiple turnovers with a 5fold molar excess of 5-amino-1-(5-phospho-D-ribosyl)imidazole
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
4-amino-2-methyl-5-phosphomethylpyrimidine is sequentially phosphorylated and combined with 4-methyl-5-(2-hydroxyethyl)-thiazole phosphate to generate thiamine monophosphate before a final phosphorylation generates the active cofactor thiamine diphosphate
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
upon interaction with S-adenosyl-L-methionine ThiC generates a persistent free radical on the alpha-carbon of an amino acid residue
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in thiamin biosynthesis
-
-
?
additional information
?
-
-
reaction assay in the anaerobic chamber
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-
?
additional information
?
-
-
reaction assay in the anaerobic chamber
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-
?
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5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in the biosynthesis of thiamine diphosphate
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in the biosynthesis of thiamine diphosphate
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
the enzyme is involved in thiamine biosynthesis
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in the biosynthesis of thiamine diphosphate
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
4-amino-2-methyl-5-phosphomethylpyrimidine is sequentially phosphorylated and combined with 4-methyl-5-(2-hydroxyethyl)-thiazole phosphate to generate thiamine monophosphate before a final phosphorylation generates the active cofactor thiamine diphosphate
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
the product 4-amino-2-methyl-5-phosphomethylpyrimidine is an intermediate of thiamine pdiphosphate (coenzyme B1) biosynthesis
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
4-amino-2-methyl-5-phosphomethylpyrimidine is sequentially phosphorylated and combined with 4-methyl-5-(2-hydroxyethyl)-thiazole phosphate to generate thiamine monophosphate before a final phosphorylation generates the active cofactor thiamine diphosphate
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
the enzyme is involved in thiamin biosynthesis
-
-
?
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evolution
-
the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily
evolution
the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily, reactions catalyzed by the radical AdoMet superfamily include mainly glycyl radical generation, sulfur insertion, methylation, methylthiolation, oxidation, isomerization, elimination (fragmentation), overview. ThiC does not contain the canonical CXXXCXXC motif in the N-terminal domain, as do most of the radical AdoMet enzymes, but a CXXCXXXXC motif
evolution
the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily, reactions catalyzed by the radical AdoMet superfamily include mainly glycyl radical generation, sulfur insertion, methylation, methylthiolation, oxidation, isomerization, elimination (fragmentation), overview. ThiC does not contain the canonical CXXXCXXC motif in the N-terminal domain, as do most of the radical AdoMet enzymes, but a CXXCXXXXC motif
evolution
-
the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily
-
malfunction
downregulation of AtTHIC expression by T-DNA insertion at its promoter region results in a drastic reduction of thiamine content in plants and the knock-down mutant thic1 shows albino (white leaves) and lethal phenotypes under the normal culture conditions
malfunction
knockdown mutant, if the thiC plants are not supplemented with thiamine, they eventually die. A concentration of 1.5 M thiamine is sufficient to allow growth of the seedlings, but these are chlorotic
malfunction
-
a compromised iron-sulfur ([Fe-S]) cluster metabolism reduces ThiC activity
malfunction
a DELTAthiC mutant displays thiamine auxotrophy, the phenotype is not due to polar mutations, as the strain is restored to wild-type growth by the expression of the corresponding thiC gene in trans
malfunction
one mechanism to allow Thi5p function in Salmonella enterica is by remodeling the metabolic network associated with the sugar phosphate stress response regulator, transcription factor SgrR (formerly YabN), integration between the sugar-phosphate stress response regulator and Thi5p activity in Salmonella enterica. SgrR belongs to a distinct class of transcription regulators (COG4533) and has a predicted N-terminal DNA-binding domain and C-terminal solute-binding domain, expression from the sgrS promoter (sgrSp) is used as a reporter of SgrR activity
malfunction
-
knockdown mutant, if the thiC plants are not supplemented with thiamine, they eventually die. A concentration of 1.5 M thiamine is sufficient to allow growth of the seedlings, but these are chlorotic
-
malfunction
-
one mechanism to allow Thi5p function in Salmonella enterica is by remodeling the metabolic network associated with the sugar phosphate stress response regulator, transcription factor SgrR (formerly YabN), integration between the sugar-phosphate stress response regulator and Thi5p activity in Salmonella enterica. SgrR belongs to a distinct class of transcription regulators (COG4533) and has a predicted N-terminal DNA-binding domain and C-terminal solute-binding domain, expression from the sgrS promoter (sgrSp) is used as a reporter of SgrR activity
-
malfunction
-
a compromised iron-sulfur ([Fe-S]) cluster metabolism reduces ThiC activity
-
malfunction
-
a DELTAthiC mutant displays thiamine auxotrophy, the phenotype is not due to polar mutations, as the strain is restored to wild-type growth by the expression of the corresponding thiC gene in trans
-
metabolism
-
the enzyme catalyzes the biosynthesis of on part of the thiamine diphosphate cofactor that is essentially used by enzymes in central metabolism such as pyruvate dehydrogenase and2-oxoglutarate dehydrogenase to stabilize the acyl carbanion
metabolism
the enzyme is important in thiamine biosynthesis, an essential compound in all living organisms that participates in several key cellular processes, such as carbohydrate and amino acid metabolism. Thiamine consists of a thiazole and a pyrimidine heterocycle, which are synthesized separately and assembled together by thiamine phosphate synthase
metabolism
the enzyme is important in thiamine biosynthesis, an essential compound in all living organisms that participates in several key cellular processes, such as carbohydrate and amino acid metabolism. Thiamine consists of a thiazole and a pyrimidine heterocycle, which are synthesized separately and assembled together by thiamine phosphate synthase
metabolism
-
the enzyme is important in thiamine diphosphate, i.e. coenzyme B1, biosynthesis
metabolism
the enzyme is important in thiamine diphosphate, vitamin B1, biosynthesis, an essential cofactor for key cellular metabolic enzymes in all forms of life
metabolism
in the archaeon Haloferax volcanii, thiamine biosynthesis is carried out by a chimera of the eukaryote-like THI4 pathway to synthesize the thiazole ring with a bacterial ThiC-like pathway to synthesize the pyrimidine (HMP) moiety. The enzyme ThiC is involved in thiamine biosynthesis. Haloferax volcanii uses a eukaryote-like Thi4 (thiamine thiazole synthase) for the production of the thiazole ring and condenses this ring with a pyrimidine moiety synthesized by an apparent bacterium-like ThiC (2-methyl-4-amino-5-hydroxymethylpyrimidine [HMP] phosphate synthase) branch. In the presence of thiamine, transcription factor ThiR represses the expression of thiC by a DNA operator sequence. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch. In archaea, thiamine biosynthesis is an apparent chimera of eukaryote- and bacterium-type pathways
metabolism
one of the mechanisms of Thi5p activation requires decreased PtsG function and an undefined role of SgrR
metabolism
ThiC catalyzes formation of HMP-P from the branch-point metabolite aminoimidazole ribotide (AIR), which is subsequently phosphorylated prior to being condensed with THZ-P to form thiamine-phosphate. Perturbation of the metabolic network in Salmonella enterica reveals cross-talk between coenzyme A and thiamine pathways connecting CoA and ThiC activity in vivo, pathways overview
metabolism
-
one of the mechanisms of Thi5p activation requires decreased PtsG function and an undefined role of SgrR
-
metabolism
-
the enzyme catalyzes the biosynthesis of on part of the thiamine diphosphate cofactor that is essentially used by enzymes in central metabolism such as pyruvate dehydrogenase and2-oxoglutarate dehydrogenase to stabilize the acyl carbanion
-
metabolism
-
in the archaeon Haloferax volcanii, thiamine biosynthesis is carried out by a chimera of the eukaryote-like THI4 pathway to synthesize the thiazole ring with a bacterial ThiC-like pathway to synthesize the pyrimidine (HMP) moiety. The enzyme ThiC is involved in thiamine biosynthesis. Haloferax volcanii uses a eukaryote-like Thi4 (thiamine thiazole synthase) for the production of the thiazole ring and condenses this ring with a pyrimidine moiety synthesized by an apparent bacterium-like ThiC (2-methyl-4-amino-5-hydroxymethylpyrimidine [HMP] phosphate synthase) branch. In the presence of thiamine, transcription factor ThiR represses the expression of thiC by a DNA operator sequence. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch. In archaea, thiamine biosynthesis is an apparent chimera of eukaryote- and bacterium-type pathways
-
physiological function
the enzyme is involved in the biosynthesis of thiamine diphosphate
physiological function
the enzyme is involved in the biosynthesis of thiamine diphosphate
physiological function
the enzyme is involved in the biosynthesis of thiamine diphosphate
physiological function
the enzyme is involved in the biosynthesis of thiamine diphosphate, the enzyme is essential for plant viability
physiological function
-
the enzyme is involved in thiamine biosynthesis
physiological function
the enzyme is involved in thiamine biosynthesis
physiological function
the enzyme ThiC is involved in thiamine biosynthesis. The archaeon Haloferax volcanii uses a eukaryote-like Thi4 (thiamine thiazole synthase) for the production of the thiazole ring and condenses this ring with a pyrimidine moiety synthesized by an apparent bacterium-like ThiC (2-methyl-4-amino-5-hydroxymethylpyrimidine [HMP] phosphate synthase) branch. In the presence of thiamine, transcription factor ThiR represses the expression of thiC by a DNA operator sequence. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch, mechanims, overview
physiological function
thiamine pyrophosphate is an essential cofactor, and is made of two independently synthesized moieties, 4-methyl-5-(2-hydroxyethyl)-thiazole phosphate (THZ-P) and 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P), the latter is synthesized involving enzyme ThiC
physiological function
-
the enzyme is involved in the biosynthesis of thiamine diphosphate, the enzyme is essential for plant viability
-
physiological function
-
the enzyme ThiC is involved in thiamine biosynthesis. The archaeon Haloferax volcanii uses a eukaryote-like Thi4 (thiamine thiazole synthase) for the production of the thiazole ring and condenses this ring with a pyrimidine moiety synthesized by an apparent bacterium-like ThiC (2-methyl-4-amino-5-hydroxymethylpyrimidine [HMP] phosphate synthase) branch. In the presence of thiamine, transcription factor ThiR represses the expression of thiC by a DNA operator sequence. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch, mechanims, overview
-
additional information
enzyme three-dimensional structure analysis and comparison, overview
additional information
-
enzyme three-dimensional structure analysis and comparison, overview
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A527T
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
D468N
-
random mutagenesis by by hydroxylamine, inactive mutant
D509G
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
D61N/G513E
-
random mutagenesis by by hydroxylamine, inactive mutant
E281K
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
G273N
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
G355D
-
random mutagenesis by by hydroxylamine, inactive mutant
G472D
-
random mutagenesis by by hydroxylamine, inactive mutant
G479R
-
random mutagenesis by by hydroxylamine, inactive mutant
G481S
-
random mutagenesis by by hydroxylamine, inactive mutant
G486D
-
random mutagenesis by by hydroxylamine, inactive mutant
G92D
-
random mutagenesis by by hydroxylamine, inactive mutant
H501Y
-
random mutagenesis by by hydroxylamine, inactive mutant
P498L
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
R397H
-
random mutagenesis by by hydroxylamine, inactive mutant
R544C
-
random mutagenesis by by hydroxylamine, inactive mutant
S247F
-
random mutagenesis by by hydroxylamine, inactive mutant
V267M
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
E281K
-
random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
-
G486D
-
random mutagenesis by by hydroxylamine, inactive mutant
-
G92D
-
random mutagenesis by by hydroxylamine, inactive mutant
-
S247F
-
random mutagenesis by by hydroxylamine, inactive mutant
-
ThiCE218K
site-directed mutagenesis, compromised ThiC variant weakly constrains the HMP pathway and the constraint is additive such that the combination of ThiCE218K or ThiCV267M with a lesion in panE prevents growth on minimal glucose medium
ThiCV267M
site-directed mutagenesis, compromised ThiC variant weakly constrains the HMP pathway and the constraint is additive such that the combination of ThiCE218K or ThiCV267M with a lesion in panE prevents growth on minimal glucose medium
M37I/A138V/G152D
site-directed mutagenesis
M37I/A138V/G152D
-
site-directed mutagenesis
-
additional information
generation of an N-terminally truncated version of Arabidopsis thaliana THIC, lacking the first 71 amino acids, a chloroplastidial targeting peptide. The truncated AtTHIC is functionally active
additional information
-
generation of an N-terminally truncated version of Arabidopsis thaliana THIC, lacking the first 71 amino acids, a chloroplastidial targeting peptide. The truncated AtTHIC is functionally active
additional information
disruption of glycolysis allows Thi5p-dependent growth on glucose. Generation of an insertion mutation in ptsG allowing Thi5p-dependent thiamine synthesis in a DELTAthiC strain, the effect of the ptsG mutation is independent of sgrS, consistent with a role for sgrS in decreasing PtsG activity. Induction of the sugar-phosphate stress response is required to decrease PtsG activity. Disrupting ptsG independently restores thiamine synthesis revealing one mechanism connecting Thi5p function and induction of the sugar-phosphate stress response
additional information
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disruption of glycolysis allows Thi5p-dependent growth on glucose. Generation of an insertion mutation in ptsG allowing Thi5p-dependent thiamine synthesis in a DELTAthiC strain, the effect of the ptsG mutation is independent of sgrS, consistent with a role for sgrS in decreasing PtsG activity. Induction of the sugar-phosphate stress response is required to decrease PtsG activity. Disrupting ptsG independently restores thiamine synthesis revealing one mechanism connecting Thi5p function and induction of the sugar-phosphate stress response
additional information
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disruption of glycolysis allows Thi5p-dependent growth on glucose. Generation of an insertion mutation in ptsG allowing Thi5p-dependent thiamine synthesis in a DELTAthiC strain, the effect of the ptsG mutation is independent of sgrS, consistent with a role for sgrS in decreasing PtsG activity. Induction of the sugar-phosphate stress response is required to decrease PtsG activity. Disrupting ptsG independently restores thiamine synthesis revealing one mechanism connecting Thi5p function and induction of the sugar-phosphate stress response
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additional information
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mutant phenotypes, overview
additional information
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mutant phenotypes, overview
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additional information
construction of strains DM13651 (zxx-8029::Tn10d(Tc) thiC1128 panE::Cm) and DM13652 (zxx-8029::Tn10d(Tc) thiC1129 panE::Cm), phenotypic analysis. Growth of representative suppressor strain DM13897 (thiC1129 panE::Cm ilvY3213) compared to parental strain DM13652 (thiC1129 panE::Cm) in minimal glucose medium: the parental thiC panE strain fails to grow on minimal glucose medium, but a suppressor derivative (DM13897) grows well. Growth of the parental strain is restored by the addition of thiamine (100 nM) or pantothenate
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expression in Escherichia coli
gene thiC, archaeal ThiC is encoded by leaderless transcripts, ruling out a riboswitch mechanism. Instead, transcription factor ThiR, that harbors an N-terminal helix-turn-helix (HTH) DNA binding domain and C-terminal ThiN (TMP synthase) domain, is identified. In the presence of thiamine, ThiR represses the expression of thiC by a DNA operator sequence that is conserved across archaeal phyla. Sequence comparisons and genetic organization analysis
gene thiC, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21AI, which also expresses Azotobacter vinelandii [Fe-S] cluster loading genes (iscSUA, hscBA, fdx, orf3, ndK)
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gene thiC, overexpression of His6-tagged enzyme from vector pET-28b(+) in a Azotobacter vinelandii strain overexpressing [Fe-S] cluster-loading genes from plasmid pDB1282
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gene thiC, recombinant expression of His-tagged N-terminally truncated mutant DELTAN71-AtTHIC in Escherichia coli strain BL21(DE3)
gene YFL058w, recombinant expression of GST-tagged enzyme mutant in Salmonella enterica strain LT2, one mechanism to allow Thi5p function in Salmonella enterica is by remodeling the metabolic network associated with the sugar phosphate stress response regulator, transcription factor SgrR (formerly YabN), integration between the sugar-phosphate stress response regulator and Thi5p activity in Salmonella enterica. SgrR belongs to a distinct class of transcription regulators (COG4533) and has a predicted N-terminal DNA-binding domain and C-terminal solute-binding domain, expression from the sgrS promoter (sgrSp) is used as a reporter of SgrR activity. Thi5p must be activated in order to function in Salmonella enterica, possibly by phosphorylation or another posttranslational modification
heterologous expression of AtTHIC can functionally complement the thiC knock-out mutant of Escherichia coli
LeThiC under the control of the cauliflower mosaic virus 35S promoter is introduced into the tl mutant by Agrobacterium tumefaciens-mediated transformation. Expression of the wild-type LeThiC gene in the tl mutant is able to complement the mutant to wild type
overexpression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
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downregulation of AtTHIC expression by T-DNA insertion at its promoter region results in a drastic reduction of thiamine content in plants and the knock-down mutant thic1 shows albino (white leaves) and lethal phenotypes under the normal culture conditions
expression of LeThiC is tightly regulated at the transcriptional and posttranscriptional level by multiple factors, such as light, Fe2+ status and thiamine diphosphate-riboswitch. A feedback regulation mechanism is involved in synthesis of the pyrimidine moiety for controlling thiamine synthesis in tomato
the abundance of LeTHIC expression is dependent on light
the expression intensity of LeThic at both the transcriptional (S form mRNA) and protein levels is increased under Fe2+ deficiency (1 or 0 mM Fe2+) compared with Fe2+ sufficiency (10 and 100 mM Fe2+), whereas no effects on LeThiC expression are observed under deficiency of Zn2+ or Mn2+
the THIC gene is negatively regulated by thiamin itself, regulation by conserved regions of mRNA that bind specific metabolites (riboswitches). As the thiamine riboswitch only responds to thiamin diphosphate but not thiamine, the down-regulation of THIC mRNA implies that the externally provided thiamine is converted to thiamine diphosphate inside the cell leading to the conformational change inducing mRNA instability
the transcript level in seedlings grown in 24 h of light is substantially higher than that in seedlings exposed to a single long day cycle (16-h light/8-h dark)
THIC transcript is not detectable two days after germination, but is readily detectable at day five
transcription factor ThiR, that harbors an N-terminal helix-turn-helix (HTH) DNA binding domain and C-terminal ThiN (TMP synthase) domain, represses the expression of thiC in presence of thiamine by a DNA operator sequence that is conserved across archaeal phyla. Despite having a ThiN domain, ThiR is catalytically inactive in compensating for the loss of ThiE (TMP synthase) function. ThiR homologs are widespread in archaea, suggesting that the regulation of these thiamine biosynthesis genes is governed by a repressor protein and not by a riboswitch or activation mechanism
the THIC gene is negatively regulated by thiamin itself, regulation by conserved regions of mRNA that bind specific metabolites (riboswitches). As the thiamine riboswitch only responds to thiamin diphosphate but not thiamine, the down-regulation of THIC mRNA implies that the externally provided thiamine is converted to thiamine diphosphate inside the cell leading to the conformational change inducing mRNA instability
the THIC gene is negatively regulated by thiamin itself, regulation by conserved regions of mRNA that bind specific metabolites (riboswitches). As the thiamine riboswitch only responds to thiamin diphosphate but not thiamine, the down-regulation of THIC mRNA implies that the externally provided thiamine is converted to thiamine diphosphate inside the cell leading to the conformational change inducing mRNA instability
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the transcript level in seedlings grown in 24 h of light is substantially higher than that in seedlings exposed to a single long day cycle (16-h light/8-h dark)
the transcript level in seedlings grown in 24 h of light is substantially higher than that in seedlings exposed to a single long day cycle (16-h light/8-h dark)
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THIC transcript is not detectable two days after germination, but is readily detectable at day five
THIC transcript is not detectable two days after germination, but is readily detectable at day five
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transcription factor ThiR, that harbors an N-terminal helix-turn-helix (HTH) DNA binding domain and C-terminal ThiN (TMP synthase) domain, represses the expression of thiC in presence of thiamine by a DNA operator sequence that is conserved across archaeal phyla. Despite having a ThiN domain, ThiR is catalytically inactive in compensating for the loss of ThiE (TMP synthase) function. ThiR homologs are widespread in archaea, suggesting that the regulation of these thiamine biosynthesis genes is governed by a repressor protein and not by a riboswitch or activation mechanism
transcription factor ThiR, that harbors an N-terminal helix-turn-helix (HTH) DNA binding domain and C-terminal ThiN (TMP synthase) domain, represses the expression of thiC in presence of thiamine by a DNA operator sequence that is conserved across archaeal phyla. Despite having a ThiN domain, ThiR is catalytically inactive in compensating for the loss of ThiE (TMP synthase) function. ThiR homologs are widespread in archaea, suggesting that the regulation of these thiamine biosynthesis genes is governed by a repressor protein and not by a riboswitch or activation mechanism
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