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.
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
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
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
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
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
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
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
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
the enzyme is important in thiamine diphosphate, vitamin B1, biosynthesis, an essential cofactor for key cellular metabolic enzymes in all forms of life
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
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
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
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
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
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
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
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
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
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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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°
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
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
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
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 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
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
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
A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica