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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[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. (338 aa)    
Predicted Functional Partners:
AEB85472.1
KEGG: ctt:CtCNB1_1659 acetolactate synthase, small subunit; TIGRFAM: Acetolactate synthase, small subunit; PFAM: Acetolactate synthase, small subunit, C-terminal; Amino acid-binding ACT.
 
 
 0.999
AEB85473.1
TIGRFAM: Acetolactate synthase, large subunit, biosynthetic; KEGG: ajs:Ajs_1769 acetolactate synthase 3 catalytic subunit; PFAM: Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, central domain.
 
 
 0.995
ilvD
TIGRFAM: Dihydroxy-acid dehydratase; KEGG: dia:Dtpsy_0987 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.993
ilvD-2
TIGRFAM: Dihydroxy-acid dehydratase; KEGG: dia:Dtpsy_0988 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family.
 
 
 0.990
AEB85394.1
Acetolactate synthase; KEGG: ajs:Ajs_2520 thiamine pyrophosphate protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain; Thiamine pyrophosphate enzyme, central domain; Belongs to the TPP enzyme family.
 
 
 0.984
AEB82761.1
Aconitate hydratase domain-containing protein; PFAM: Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha; Aconitase A/isopropylmalate dehydratase small subunit, swivel; KEGG: cti:RALTA_B0856 putative hydrolyase.
 
  
 0.979
AEB83428.1
Acetolactate synthase; KEGG: ajs:Ajs_3488 hypothetical protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain.
 
 
 0.977
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.
 
  
 0.886
AEB83473.1
Homoaconitate hydratase family protein; KEGG: xtr:100490803 isopropylmalate/citramalate isomerase large subunit-like; TIGRFAM: Homoaconitase/3-isopropylmalate dehydratase, large subunit, subgroup; PFAM: Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha.
 
  
 0.878
AEB83472.1
KEGG: reu:Reut_B4842 3-isopropylmalate dehydratase, small subunit; TIGRFAM: 3-isopropylmalate dehydratase, small subunit, subgroup; PFAM: Aconitase A/isopropylmalate dehydratase small subunit, swivel; Belongs to the LeuD family.
 
  
 0.865
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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