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thiOFAD-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 interm [...] (369 aa)    
Predicted Functional Partners:
thiG
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.
 
 0.999
thiF
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; Belongs to the HesA/MoeB/ThiF family.
 
  
 0.993
tenI
Thiazole tautomerase; 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.
 
  
 0.983
thiD
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.
  
  
 0.983
thiS
Sulfur carrier for synthesis of hydroxyethylthiazole phosphate; Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate; Belongs to the sulfur carrier protein ThiS family.
  
  
 0.977
gcvT
Aminomethyltransferase (glycine cleavage system protein T); The glycine cleavage system catalyzes the degradation of glycine.
 
 
 0.966
tenA
Thiaminase II; 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 products present in the enviro [...]
  
  
 0.954
thiE
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. Belongs to the thiamine-phosphate synthase family.
     
 0.859
thiX
Thiamine transporter, permease component; Part of the ABC transporter complex YkoCDEF that could transport hydroxymethylpyrimidine (HMP) and/or thiamine. Could also transport other HMP-containing products. Probably responsible for the translocation of the substrate across the membrane (Probable).
 
  
 0.802
thiL
tRNA-Asp; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.
      
 0.771
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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