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thrC protein (Bacillus cereus) - STRING interaction network
"thrC" - Threonine synthase in Bacillus cereus
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine (352 aa)    
Predicted Functional Partners:
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily (297 aa)
 
 
  0.999
hom_1
annotation not available (394 aa)
 
   
  0.996
hom_2
annotation not available (431 aa)
 
   
  0.987
serC
Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily (360 aa)
     
  0.967
DJ87_2868
annotation not available (37 aa)
   
   
  0.955
ilvA_1
L-threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (420 aa)
   
 
0.923
tdcB
L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (333 aa)
   
 
0.923
asd_1
asd_B- aspartate-semialdehyde dehydrogenase (347 aa)
   
 
  0.834
asd_2
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L- aspartyl-4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family (348 aa)
   
 
  0.834
hom_3
annotation not available (346 aa)
 
   
  0.781
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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