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second shell of interactors
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AGB15048.1Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (421 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.
 
 
 0.985
AGB14822.1
Threonine dehydratase, medium form; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form.
  
 
0.939
AGB17138.1
Threonine dehydratase, medium form; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form.
  
 
0.939
AGB15031.1
Threonine aldolase; PFAM: Beta-eliminating lyase.
  
 0.923
AGB17147.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
  
  
 
0.919
AGB15365.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
  
  
 
0.914
AGB17002.1
PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase.
 
 
 0.841
AGB17753.1
Aspartokinase; PFAM: Amino acid kinase family; TIGRFAM: aspartate kinase; Belongs to the aspartokinase family.
  
 
 0.762
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
  
  
 0.757
pdxS
Pyridoxine biosynthesis enzyme; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
  
    0.711
Your Current Organism:
Halovivax ruber
NCBI taxonomy Id: 797302
Other names: H. ruber XH-70, Halovivax ruber JCM 13892, Halovivax ruber XH-70, Halovivax ruber str. XH-70, Halovivax ruber strain XH-70
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