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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
leuB3-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. (360 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.
 0.999
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 1 subfamily.
 
 0.998
hom
Homoserine dehydrogenase.
  
 
 0.987
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.
 
  
 0.952
ilvH
Acetolactate synthase isozyme 3 small subunit.
 
 
 0.938
ilvD
Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
 
  
 0.929
leuA
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. LeuA type 2 subfamily.
 
 0.917
araC_2
L-arabonate dehydratase; Belongs to the IlvD/Edd family.
 
  
 0.894
ilvI
Acetolactate synthase isozyme 3 large subunit.
 
 0.894
nuoC
NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
  
 
 0.838
Your Current Organism:
Pseudomonas fluorescens
NCBI taxonomy Id: 294
Other names: ATCC 13525, Bacillus fluorescens, Bacillus fluorescens liquefaciens, Bacterium fluorescen, CCEB 546, CFBP 2102, CIP 69.13, DSM 50090, IAM 12022, IFO 14160, JCM 5963, Liquidomonas fluorescens, NBRC 14160, NCCB 76040, NCIB 9046, NCIB:9046, NCIMB 9046, NCTC 10038, NRRL B-14678, P. fluorescens, Pseudomonas sp. AU2390, Pseudomonas sp. BZ64, Pseudomonas sp. FY32, Pseudomonas sp. HSA2/2016, Pseudomonas sp. HSA3/2016, Pseudomonas sp. ISSDS-433, Pseudomonas sp. JCM 17186, Pseudomonas sp. JCM 2779, Pseudomonas sp. KH-20150KS3, Pseudomonas sp. LBUM223, Pseudomonas sp. LBUM636, Pseudomonas sp. SM2/2016, RH 818, VKM B-894, bacterium P1-1, strain M. Rhodes 28/5
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