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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
AEB83747.1TIGRFAM: Tartrate dehydrogenase; KEGG: ajs:Ajs_1120 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase. (355 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.
  
 0.975
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.
 
 0.954
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.
 
 0.952
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.
  
 0.944
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.
  
 0.944
AEB84100.1
TIGRFAM: Tartrate dehydrogenase; KEGG: aav:Aave_2087 tartrate dehydrogenase; PFAM: Isocitrate/isopropylmalate dehydrogenase.
  
  
 
0.905
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.
 
 0.842
AEB86262.1
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
 0.809
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.
  
  
 0.777
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 
 0.767
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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