bifunctional thiamine phosphate synthase (TP synthase or ThiE)/hydroxyethylthiazole kinase (ThZ kinase or ThiM) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole, and the phosphorylation of the hydroxylgroup of 4-methyl-5-beta-hydroxyethylthiazole, in the thiamine biosynthesis pathway
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
264-530
1.48e-91
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
The actual alignment was detected with superfamily member TIGR00694:
Pssm-ID: 469648 [Multi-domain] Cd Length: 249 Bit Score: 280.40 E-value: 1.48e-91
hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a ...
264-530
1.48e-91
hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a number of bacteria, and C-terminal domains of bifunctional thiamine biosynthesis proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the N-terminal domain corresponds to the bacterial thiamine-phosphate pyrophosphorylase (EC 2.5.1.3), ThiE. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 188074 [Multi-domain] Cd Length: 249 Bit Score: 280.40 E-value: 1.48e-91
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
262-522
1.28e-84
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.
Pssm-ID: 238575 [Multi-domain] Cd Length: 242 Bit Score: 262.48 E-value: 1.28e-84
Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; ...
251-527
2.88e-71
Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; Hydroxyethylthiazole kinase, sugar kinase family is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441748 [Multi-domain] Cd Length: 264 Bit Score: 228.45 E-value: 2.88e-71
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
11-225
1.88e-70
thiamine-phosphate diphosphorylase; 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. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 224.05 E-value: 1.88e-70
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
12-226
1.58e-67
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, 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. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 216.23 E-value: 1.58e-67
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) 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. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. 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.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 207.01 E-value: 3.41e-64
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
9-232
6.04e-64
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 207.35 E-value: 6.04e-64
hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a ...
264-530
1.48e-91
hydroxyethylthiazole kinase; This model represents the hydoxyethylthiazole kinase, ThiM, of a number of bacteria, and C-terminal domains of bifunctional thiamine biosynthesis proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the N-terminal domain corresponds to the bacterial thiamine-phosphate pyrophosphorylase (EC 2.5.1.3), ThiE. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 188074 [Multi-domain] Cd Length: 249 Bit Score: 280.40 E-value: 1.48e-91
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
262-522
1.28e-84
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.
Pssm-ID: 238575 [Multi-domain] Cd Length: 242 Bit Score: 262.48 E-value: 1.28e-84
Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; ...
251-527
2.88e-71
Hydroxyethylthiazole kinase, sugar kinase family [Coenzyme transport and metabolism]; Hydroxyethylthiazole kinase, sugar kinase family is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441748 [Multi-domain] Cd Length: 264 Bit Score: 228.45 E-value: 2.88e-71
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
11-225
1.88e-70
thiamine-phosphate diphosphorylase; 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. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 224.05 E-value: 1.88e-70
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
12-226
1.58e-67
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, 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. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 216.23 E-value: 1.58e-67
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) 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. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. 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.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 207.01 E-value: 3.41e-64
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
9-232
6.04e-64
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 207.35 E-value: 6.04e-64
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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