InterPro domain: IPR034291

Thiamine phosphate synthase (TPS), also known as thiamin phosphate pyrophosphorylase (TMP-PPase), catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate in the thiamine biosynthesis pathway [ 1 ]. This family includes the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria [ 2 ], and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase ThiM [ 3 ]. The plant enzyme is also bifunctional [ 4 ].

1. Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis. J. Bacteriol. 179, 3030-5
2. Thiamin biosynthesis in prokaryotes. Arch. Microbiol. 171, 293-300
3. Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae. J. Biol. Chem. 269, 30510-6
4. A Brassica cDNA clone encoding a bifunctional hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase involved in thiamin biosynthesis. Plant Mol. Biol. 37, 955-66