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ilvE ilvE ilvD ilvD leuA leuA leuA-2 leuA-2 AGA87622.1 AGA87622.1 ilvA ilvA AGA88005.1 AGA88005.1 panB panB AGA86321.1 AGA86321.1 gshA gshA AGA86853.1 AGA86853.1
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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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ilvEBranched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (307 aa)    
Predicted Functional Partners:
ilvD
PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
  
 0.992
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
 
 0.991
leuA-2
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
  
 0.989
AGA87622.1
PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain.
  
 0.976
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.
  
 
 0.946
AGA88005.1
PFAM: Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glu/Leu/Phe/Val dehydrogenase, dimerisation domain; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
  
 
 0.930
panB
Ketopantoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate; Belongs to the PanB family.
    
 0.922
AGA86321.1
PFAM: Aminotransferase class I and II.
  
 
 0.916
gshA
PFAM: Glutamate-cysteine ligase; TIGRFAM: glutamate--cysteine ligase; Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily.
     
  0.900
AGA86853.1
PFAM: haloacid dehalogenase-like hydrolase; TIGRFAM: phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein.
    
 0.852
Your Current Organism:
Pseudomonas stutzeri
NCBI taxonomy Id: 644801
Other names: P. stutzeri RCH2, Pseudomonas stutzeri RCH2, Pseudomonas stutzeri str. RCH2, Pseudomonas stutzeri strain RCH2
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