EC Number |
General Information |
Reference |
---|
4.1.99.17 | evolution |
the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily |
-, 727762 |
4.1.99.17 | 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 |
727883 |
4.1.99.17 | malfunction |
a compromised iron-sulfur ([Fe-S]) cluster metabolism reduces ThiC activity |
-, 727762 |
4.1.99.17 | 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 |
-, 748112 |
4.1.99.17 | 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 |
714680 |
4.1.99.17 | 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 |
-, 716741 |
4.1.99.17 | 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 |
-, 748101 |
4.1.99.17 | 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 |
-, 748112 |
4.1.99.17 | metabolism |
one of the mechanisms of Thi5p activation requires decreased PtsG function and an undefined role of SgrR |
-, 748101 |
4.1.99.17 | 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 |
-, 727762 |