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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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AEH23003.1KEGG: tye:THEYE_A0114 3-isopropylmalate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. (359 aa)    
Predicted Functional Partners:
leuC
3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.998
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.
 
 0.998
AEH23480.1
KEGG: dak:DaAHT2_0726 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
  
 0.987
AEH23479.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: dsa:Desal_2398 acetolactate synthase, large subunit, biosynthetic type; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP binding region; Thiamine pyrophosphate enzyme, central region; Thiamine pyrophosphate enzyme, C-terminal TPP-binding.
 
 0.962
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.
  
  
 0.931
ilvD
PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; HAMAP: Dihydroxy-acid dehydratase; KEGG: dak:DaAHT2_2250 dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
  
 0.912
uvrC
UvrABC system protein C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
       0.798
AEH23514.1
TIGRFAM: Isocitrate dehydrogenase NADP-dependent, prokaryotic; KEGG: sfu:Sfum_3896 isocitrate dehydrogenase, NADP-dependent; PFAM: Isocitrate/isopropylmalate dehydrogenase.
 
 
0.732
AEH22324.1
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.
  
 
 0.711
AEH22825.1
TIGRFAM: 2-isopropylmalate synthase/homocitrate synthase related; KEGG: sfu:Sfum_2174 putative alpha-isopropylmalate/homocitrate synthase family transferase; PFAM: 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; Pyruvate carboxyltransferase; Belongs to the alpha-IPM synthase/homocitrate synthase family.
  
 
 0.711
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
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