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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
white nodes:
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
AMS41455.1Serine dehydratase; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme. (304 aa)    
Predicted Functional Partners:
AMS43730.1
Pfam:pfam14821 Threonine synthase N terminus.
 
 
 0.951
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.
 
 0.948
AMS41792.1
Acetolactate synthase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.
 
 0.945
AMS39617.1
Putative 2-ketoarginine decarboxylase AruI; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family.
 
 0.942
AMS41793.1
Pfam:pfam10369 Small subunit of acetolactate synthase.
  
 0.940
AMS41690.1
Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Belongs to the TPP enzyme family.
 
 0.938
AMS43989.1
Threonine synthase-like protein; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
  
 
0.931
AMS40117.1
Decarboxylase; Pfam:pfam02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain.
  
 0.930
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.928
ilvA
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.
  
  
 
0.926
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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