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cimA cimA leuC leuC leuD leuD ilvH ilvH ilvB ilvB MJ_0663 MJ_0663 leuB leuB hacB hacB korA korA porA porA porB porB
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query proteins and first shell of interactors
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second shell of interactors
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Predicted Interactions
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textmining
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protein homology
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cimA2-isopropylmalate synthase (leuA); Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate; Belongs to the alpha-IPM synthase/homocitrate synthase family. (491 aa)    
Predicted Functional Partners:
leuC
3-isopropylmalate dehydratase (leuC); Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate; Belongs to the [...]
 
 
 0.973
leuD
3-isopropylmalate dehydratase (leuD); Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.
  
 
 0.972
ilvH
Acetolactate synthase small subunit (ilvN); Similar to GB:L03181 SP:P37252 PID:143092 PID:1770067 GB:AL009126 percent identity: 49.37; identified by sequence similarity; putative; Belongs to the acetolactate synthase small subunit family.
  
 
 0.963
ilvB
Acetolactate synthase large subunit (ilvB); Similar to GB:L03181 SP:P37251 PID:143091 percent identity: 50.18; identified by sequence similarity; putative; Belongs to the TPP enzyme family.
  
 
 0.948
MJ_0663
Acetolactate synthase large subunit (ilvB); Similar to GB:L10328 SP:P08142 GB:J01633 GB:X02541 PID:146455 percent identity: 30.21; identified by sequence similarity; putative; Belongs to the TPP enzyme family.
  
 
 0.946
leuB
3-isopropylmalate dehydrogenase 1 (leuB1); Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate, which decarboxylates to 4-methyl-2-oxopentanoate (2- oxoisocaproate). Also catalyzes the oxidative decarboxylation of 3- methylmalate to 2-oxobutyrate, and that of D-malate to pyruvate. Cannot use NADP(+) instead of NAD(+). Cannot catalyze the oxidation of L- malate, L-tartrate, D-tartrate, DL-isocitrate, or DL-lactate.
 
 
 0.911
hacB
3-isopropylmalate dehydratase (leuD); Hydro-lyase with broad substrate specificity for cis- unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)- aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are pa [...]
  
 
 0.870
korA
2-ketoglutarate ferredoxin oxidoreductase, subunit alpha (korA); Similar to GB:X64521 PID:43498 percent identity: 44.24; identified by sequence similarity; putative.
  
 
 0.843
porA
Pyruvate ferredoxin oxidoreductase, subunit alpha (porA); Similar to PID:1197363 percent identity: 57.33; identified by sequence similarity; putative.
  
 
 0.838
porB
Pyruvate ferredoxin oxidoreductase, subunit beta (porB); Similar to PID:1197364 percent identity: 58.89; identified by sequence similarity; putative.
  
 
 0.837
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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