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Enzyme Nomenclature
Information on EC 4.1.99.17 - phosphomethylpyrimidine synthase
for references in articles please use BRENDA:EC4.1.99.17
Word Map on EC 4.1.99.17
- 4.1.99.17
- thiamin
-
5\'-deoxyadenosyl
- pyrophosphate
- ribotide
-
entitled
-
barrel
- ribonucleotide
-
periplasmic
- 5-aminoimidazole
- 5'-deoxyadenosine
- thiazole
- s-adenosylmethionine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
4.1.99.17
-
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RECOMMENDED NAME
GeneOntology No.
phosphomethylpyrimidine synthase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
radical reaction mechanism, overview
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
radical reaction mechanism, overview
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 a [4Fe-4S] cluster to reductively cleave AdoMet to methionine and a 5'-deoxyadenosyl radical that initiates catalysis
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
5-amino-1-(5-phospho-D-ribosyl)imidazole formate-lyase (decarboxylating, 4-amino-2-methyl-5-phosphomethylpyrimidine-forming)
Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The first stage of catalysis is reduction of the S-adenosyl-L-methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate. Part of the pathway for thiamine biosynthesis.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
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
-
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
-
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
-
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 thiamine biosynthesis
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 the biosynthesis of thiamine diphosphate, the enzyme is essential for plant viability
-
additional information
-
enzyme three-dimensional structure analysis and comparison, overview
additional information
enzyme three-dimensional structure analysis and comparison, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
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 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
-
-
-
-
?
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
-
-
-
additional information
?
-
-
reaction assay in the anaerobic chamber
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
O82392
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
O82392
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
O82392
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
Q9A6Q5
-
-
-
?
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
Q9A6Q5
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
Q9L9I7
-
-
-
?
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
B9TU32
the enzyme is involved in thiamin biosynthesis
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4Fe-4S-center
-
ThiC carries an oxygen labile [Fe-S] cluster essential for activity
S-adenosyl-L-methionine
a S-adenosyl-L-methionine radical enzyme
S-adenosyl-L-methionine
-
a S-adenosyl-L-methionine radical enzyme. ThiC uses AdoMet as an oxidizing cosubstrate in 1:1 stoichiometry
[4Fe-4S]-center
binds 1 4Fe-4S cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4Fe-4S center
binds 1 4Fe-4S cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine
4Fe-4S cluster
Co2+
a metal ion with octahedral coordination (two strictly conserved histidine residues (H426 and H490) and four water molecules) at the same location as a zinc ion in the bacterial enzyme, and a metal ion with multiple coordinated water molecules in the close vicinity of the substrate binding sites, binding structures, overview
Fe2+
iron-sulfur centre
4Fe-4S cluster
-
ThiC carries an oxygen labile [Fe-S] cluster essential for activity
Fe2+
the enzyme contains a [4Fe-4S] cluster bound by the CXXCXXXXC motif
Fe2+
the enzyme contains a [4Fe-4S] cluster bound by the CXXCXXXXC motif
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
inhibitiory potencies, overview. No inhibition by product 4-amino-2-methyl-5-phosphomethylpyrimidine, and by cAMP, ADP, ATP, imidazole, aminoimidazole carboxamide ribotides, 5-amino-4-imidazolecarboxylic acid ribotide, CoA, acetyl-CoA, adenine, and 2'-deoxyadenosine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
5-amino-1-(5-phospho-D-ribosyl)imidazole
-
pH 8.0, 37°C, recombinant His-tagged enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
ThiC undergoes ThiC undergoes steady-state turnover, and multiple turnovers with a 5fold molar excess of 5-amino-1-(5-phospho-D-ribosyl)imidazole
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics, overview
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Caulobacter vibrioides (strain ATCC 19089 / CB15)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65451
2 * 65451, recombinant His-tagged DELTAN71-AtTHIC mutant, mass spectrometry and crystal structure
130000
recombinant His-tagged DELTAN71-AtTHIC mutant, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 65451, recombinant His-tagged DELTAN71-AtTHIC mutant, mass spectrometry and crystal structure
additional information
additional information
-
enzyme three-dimensional structure analysis, overview
additional information
enzyme three-dimensional structure analysis, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged DELTAN71-AtTHIC mutant, by a proteolysis assay (especially alpha-chymotrypsin) coupled with the sitting drop vapor diffusion technique at 18°C, using 0.01 M cobalt (II) chloride hexahydrate, 0.1 M sodium acetate trihydrate, pH 4.6, 1 M 1,6-hexanediol, X-ray diffraction structure determination and analysis at 1.6 A resolution
selenomethionine HMP-P synthase/HMP crystals are grown using the sitting drop vapor diffusion method at 25°C. The crystals are monoclinic, space group P2(1), with unit cell dimension a = 63.3 A, b = 103.4 A, c = 95.4 A and beta = 91.6°
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
-
purified recombinant His-tagged wild-type and mutant enzymes, 3 min, inactivation
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
identification of variants of ThiC that have increased sensitivity to oxidative growth conditions
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716133
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged N-terminally truncated mutant DELTAN71-AtTHIC from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21AI by nickel affinity chromatography and gel filtration
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recombinant His6-tagged enzyme from Azotobacter vinelandii, the [4Fe-4S] cluster is reconstituted in vitro prior to freezing of the enzyme at -80°C
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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)
heterologous expression of AtTHIC can functionally complement the thiC knock-out mutant of Escherichia coli
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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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
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 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); THIC transcript is not detectable two days after germination, but is readily detectable at day five
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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); THIC transcript is not detectable two days after germination, but is readily detectable at day five
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A527T
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
D509G
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
E281K
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
G273N
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
P498L
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
V267M
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
E281K
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random mutagenesis by by hydroxylamine, the mutant shows reduced activity compared to the wild-type enzyme
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additional information
additional information
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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
Show AA Sequence (12458 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.99.17)
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