STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Gene Fusion
Cooccurrence
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[Homology]
Score
ilvCKetol-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. (331 aa)    
Predicted Functional Partners:
AEM77529.1
KEGG: tbo:Thebr_0013 acetolactate synthase small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
 
 
 0.999
AEM77536.1
KEGG: tit:Thit_0020 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, central region; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
 
 
 0.999
ilvD
TIGRFAM: Dihydroxy-acid dehydratase; HAMAP: Dihydroxy-acid dehydratase; KEGG: tit:Thit_0019 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.998
AEM79120.1
KEGG: cce:Ccel_1264 dihydroxy-acid and 6-phosphogluconate dehydratase; manually curated; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.995
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.
 
  
 0.992
leuD
3-isopropylmalate dehydratase 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.
 
  
 0.991
leuC
3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
  
 0.989
AEM77531.1
PFAM: Pyruvate carboxyltransferase; KEGG: tbo:Thebr_0015 pyruvate carboxyltransferase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
  
 0.967
AEM77992.1
KEGG: tmt:Tmath_0527 homocitrate synthase; TIGRFAM: Homocitrate synthase NifV-type; PFAM: Pyruvate carboxyltransferase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
  
 0.818
AEM79167.1
KEGG: thx:Thet_1706 2-isopropylmalate synthase/homocitrate synthase family protein; TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase related; PFAM: Pyruvate carboxyltransferase; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
  
 0.797
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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