STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
tenIThiazole tautomerase (transcriptional regulator teni); Catalyzes the irreversible aromatization of 2-((2R,5Z)-2- carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate (cThz*-P) to 2- (2-carboxy-4-methylthiazol-5-yl)ethyl phosphate (cThz-P), a step in the biosynthesis of the thiazole phosphate moiety of thiamine. Cannot use cThz* as substrate, indicating that the phosphate group is essential. Has no thiamine phosphate synthase activity, despite a high sequence similarity with ThiE (205 aa)    
Predicted Functional Partners:
Hydroxyethylthiazole phosphate synthetase (thiamine biosynthesis); Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S
Thiaminase (transcriptional activator tena); Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4- amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2- methylpyrimidine (HMP). To a lesser extent, is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity is unlikely to be physiologically relevant. Therefore, is involved in the regeneration of the thiamine pyrimidine from thiamine degraded [...]
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine
Adenylate transferase and sulfur transferase (thiamine biosynthesis); Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS
Fad-dependent glycine oxidase; Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N- methylglycine), N-ethylglycine and glycine Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine) . Displays lower activities on D-alanine, D-valine, D-proline and D-methionine . Does not act on L-amino acids and other D-amino acids . Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine inte [...]
Phosphorylates B6 vitamers; functions in a salvage pathway. Uses pyridoxal, pyridoxine, and pyridoxamine as substrates. Can also use hydroxymethylpyrimidine (HMP) as substrate
Sulfur carrier for synthesis of hydroxyethylthiazole phosphate; Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP
Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ)
Biosynthesis of the pyrimidine moiety from 5-aminoimidazole ribotide (air) (thiamin biosynthesis); Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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