Nodes:
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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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[Homology]
Score
Meso_0309L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: ret:RHE_CH03537 probable threonine dehydratase protein. (324 aa)    
Predicted Functional Partners:
leuB
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
 
 0.949
Meso_1489
TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit.
  
 0.942
Meso_0760
TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: mlo:mll7517 threonine synthase.
  
 
 0.937
Meso_1062
Acetolactate synthase, large subunit; PFAM: thiamine pyrophosphate enzyme-like TPP-binding thiamine pyrophosphate enzyme, central region thiamine pyrophosphate enzyme-like TPP binding region; KEGG: bme:BMEII0351 acetolactate synthase large subunit.
 
 0.933
Meso_3590
Acetolactate synthase, large subunit; PFAM: thiamine pyrophosphate enzyme-like TPP-binding thiamine pyrophosphate enzyme, central region thiamine pyrophosphate enzyme-like TPP binding region; KEGG: ret:RHE_PF00274 acetolactate synthase, large subunit protein (thiamine pyrophosphate-dependent enzyme).
 
 0.933
Meso_2037
PFAM: thiamine pyrophosphate enzyme-like TPP-binding thiamine pyrophosphate enzyme, central region thiamine pyrophosphate enzyme-like TPP binding region; KEGG: mlo:mlr1615 acetolactate synthase large subunit.
 
 0.932
trpB
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.928
ilvA
L-threonine ammonia-lyase; 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.
  
  
 
0.924
Meso_0823
PFAM: thiamine pyrophosphate enzyme-like TPP-binding thiamine pyrophosphate enzyme, central region thiamine pyrophosphate enzyme-like TPP binding region; KEGG: thiamine pyrophosphate-requiring enzyme; Belongs to the TPP enzyme family.
  
 0.923
Meso_1488
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme-like TPP-binding thiamine pyrophosphate enzyme, central region thiamine pyrophosphate enzyme-like TPP binding region; KEGG: mlo:mll1433 acetolactate synthase large subunit.
  
 0.923
Your Current Organism:
Chelativorans sp. BNC1
NCBI taxonomy Id: 266779
Other names: C. sp. BNC1, Mesorhizobium sp. BNC1
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