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ilvD ilvD ilvC ilvC leuA leuA ilvE ilvE ACS42657.1 ACS42657.1 ACS41918.1 ACS41918.1 ilvA ilvA panB panB leuC leuC ilvD-2 ilvD-2 leuD leuD
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query proteins and first shell of interactors
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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
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gene co-occurrence
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textmining
co-expression
protein homology
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ilvDDihydroxyacid dehydratase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family. (611 aa)    
Predicted Functional Partners:
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.
 
 
 0.992
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.
 
 
 0.992
ilvE
Putative branched-chain amino acid transferase (ilvE-like); Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
 0.977
ACS42657.1
Putative branched-chain amino acid aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 0.977
ACS41918.1
Putative branched-chain amino acid aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 0.965
ilvA
Threonine deaminase; 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.
  
 0.931
panB
3-methyl-2-oxobutanoate hydroxymethyltransferase, pantothenate biosynthetic process; 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.
     
 0.919
leuC
3-isopropylmalate isomerase, subunit with LeuD; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.912
ilvD-2
Putative dihydroxyacid dehydratase (ilvD-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the IlvD/Edd family.
  
  
 
0.904
leuD
Isopropylmalate dehydratase small subunit/isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.903
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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