Protein Family Models

Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyses 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 [1]. This Pfam family also includes the regulatory protein TENI (Swiss:P25053), a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production [2]. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase [3]. [1]. 9139923. Characterization of the Bacillus subtilis thiC operon involved. in thiamine biosynthesis.. Zhang Y, Taylor SV, Chiu HJ, Begley TP;. J Bacteriol 1997;179:3030-3035.. [2]. 1898926. Cloning and characterization of a pair of novel genes that. regulate production of extracellular enzymes in Bacillus. subtilis.. Pang AS, Nathoo S, Wong SL;. J Bacteriol 1991;173:46-54.. [3]. 21534620. A missing enzyme in thiamin thiazole biosynthesis:. identification of TenI as a thiazole tautomerase.. Hazra AB, Han Y, Chatterjee A, Zhang Y, Lai RY, Ealick SE,. Begley TP;. J Am Chem Soc. 2011;133:9311-9319. (from Pfam)

Date:

2024-08-14

thiamine phosphate synthase (TP synthase) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole in the thiamine biosynthesis pathway

Date:

2023-03-02

This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, 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 (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI.

Gene:

thiE

Date:

2021-04-27