Nodes:
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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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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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experimentally determined
co-expression
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gene co-occurrence
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[Homology]
Score
FAD_15892-isopropylmalate synthase; Belongs to the alpha-IPM synthase/homocitrate synthase family. (345 aa)    
Predicted Functional Partners:
hicdh
Homoisocitrate dehydrogenase.
 
 
 0.841
FAD_1590
Carnitine dehydratase.
  
 
 0.813
lysT
Homoaconitase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.694
FAD_1789
3-isopropylmalate dehydratase large subunit.
 
  
 0.663
lysU
Homoaconitase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 2 subfamily.
 
  
 0.661
FAD_1591
Major facilitator superfamily permease.
       0.604
FAD_1790
3-isopropylmalate dehydratase small subunit.
  
  
 0.552
FAD_1250
Acetolactate synthase catalytic subunit.
  
 
 0.546
FAD_1592
Transposase.
       0.544
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.
  
  
 0.539
Your Current Organism:
Ferroplasma acidiphilum
NCBI taxonomy Id: 74969
Other names: DSM 12658, F. acidiphilum, Ferromonas metallovorans, Ferroplasma acidiphilum Golyshina et al. 2000, JCM 10970
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