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
Your Input:
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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. (330 aa)    
Predicted Functional Partners:
AEG58655.1
TIGRFAM: acetolactate synthase, small subunit; KEGG: drm:Dred_0282 acetolactate synthase 3 regulatory subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein.
 
 
 0.999
AEG58654.1
KEGG: drm:Dred_0281 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein.
 
 
 0.998
ilvD
TIGRFAM: dihydroxy-acid dehydratase; KEGG: drm:Dred_0280 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.997
AEG58657.1
KEGG: drm:Dred_0284 acetolactate synthase, large subunit, biosynthetic type; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein.
 
 
 0.996
AEG59017.1
KEGG: drm:Dred_2896 acetolactate synthase 3 regulatory subunit; TIGRFAM: acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit-like; amino acid-binding ACT domain protein.
 
 
 0.994
ilvD-2
TIGRFAM: dihydroxy-acid dehydratase; KEGG: aar:Acear_1923 dihydroxyacid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.994
ilvD-3
TIGRFAM: dihydroxy-acid dehydratase; KEGG: ccb:Clocel_0493 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.994
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.
 
  
 0.936
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.
 
  
 0.935
AEG59106.1
KEGG: drm:Dred_2805 glutamate synthase (ferredoxin); PFAM: glutamine amidotransferase class-II; glutamate synthase; ferredoxin-dependent glutamate synthase; glutamate synthase alpha subunit domain protein.
  
  
 0.883
Your Current Organism:
Desulfotomaculum ruminis
NCBI taxonomy Id: 696281
Other names: D. ruminis DSM 2154, Desulfotomaculum ruminis ATCC 23193, Desulfotomaculum ruminis DL, Desulfotomaculum ruminis DSM 2154, Desulfotomaculum ruminis str. DSM 2154, Desulfotomaculum ruminis strain DSM 2154
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.