CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.20 | Alpha-Beta Barrel | |
3.20.20 | TIM Barrel | |
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
Superfamily | Aldolase class I |
Functional Family | Thiamine-phosphate synthase |
Enzyme Information
2.5.1.3 |
Thiamine phosphate synthase.
based on mapping to UniProt Q8U192
(1) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy- 4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (2) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4- methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (3) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
-!- The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. -!- The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate. -!- However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. -!- In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products. -!- In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme.
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UniProtKB Entries (1)
Q8U192 |
THIE_PYRFU
Pyrococcus furiosus DSM 3638
Thiamine-phosphate synthase
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PDB Structure
PDB | 1XI3 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Thiamine phosphate pyrophosphorylase from Pyrococcus furiosus Pfu-1255191-001
To be published
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