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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
metXHomoserine O-acetyltransferase; Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. (381 aa)    
Predicted Functional Partners:
metW
metW: methionine biosynthesis protein MetW.
  
 0.998
mdeA_2
OAH_OAS_sulfhy: O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein.
 
 
 0.991
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
 
  
 0.969
hom
Homoserine dehydrogenase.
 
 0.956
yggG_2
Peptidase M48 family protein.
       0.866
glyA2_1
Beta-eliminating lyase family protein; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
     
 0.839
glyA2
Serine hydroxymethyltransferase 2; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
     
 0.839
psdht
Phenylserine dehydratase.
  
 
 0.836
ilvA
Threonine ammonia-lyase, biosynthetic; 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.
  
 
 0.836
ilvA-2
Threonine ammonia-lyase, biosynthetic; 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.
  
 
 0.836
Your Current Organism:
Burkholderia oklahomensis
NCBI taxonomy Id: 342113
Other names: B. oklahomensis, Burkholderia oklahomensis Glass et al. 2006, CCUG 51349, DSM 21774, LMG 23618, LMG:23618, NCTC 13387, strain C6786
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