4.1.99.17: phosphomethylpyrimidine synthase
This is an abbreviated version!
For detailed information about phosphomethylpyrimidine synthase, go to the full flat file.
Word Map on EC 4.1.99.17
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4.1.99.17
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thiamin
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pyrophosphate
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enterica
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5\'-deoxyadenosyl
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thiazole
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iron-sulfur
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salvage
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fe-s
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pyridoxal
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5'-phosphate
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ribotide
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barrel
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auxotrophy
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ribonucleotide
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5'-deoxyadenosine
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single-turnover
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entitled
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5-aminoimidazole
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tpp
- 4.1.99.17
- thiamin
- pyrophosphate
- enterica
-
5\'-deoxyadenosyl
- thiazole
-
iron-sulfur
-
salvage
- fe-s
- pyridoxal
- 5'-phosphate
- ribotide
-
barrel
-
auxotrophy
- ribonucleotide
- 5'-deoxyadenosine
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single-turnover
-
entitled
- 5-aminoimidazole
- tpp
Reaction
Synonyms
2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate synthase, 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase, AtTHIC, HMP phosphate synthase, HMP-P synthase, LeThiC, Thi5p, thiC
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General Information
General Information on EC 4.1.99.17 - phosphomethylpyrimidine synthase
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evolution
malfunction
metabolism
physiological function
additional information
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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
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the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily
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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
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
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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
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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
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malfunction
Saccharomyces cerevisiae ATCC 204508 / S288c
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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
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malfunction
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a compromised iron-sulfur ([Fe-S]) cluster metabolism reduces ThiC activity
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malfunction
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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
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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
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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
Saccharomyces cerevisiae ATCC 204508 / S288c
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one of the mechanisms of Thi5p activation requires decreased PtsG function and an undefined role of SgrR
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metabolism
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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
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metabolism
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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
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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 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
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the enzyme is involved in the biosynthesis of thiamine diphosphate, the enzyme is essential for plant viability
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physiological function
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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
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enzyme three-dimensional structure analysis and comparison, overview
additional information
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enzyme three-dimensional structure analysis and comparison, overview