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
OME90001.1Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (161 aa)    
Predicted Functional Partners:
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.
 
 
 0.999
IlvB-2
Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
IlvB
FAD-dependent oxidoreductase; Incomplete; partial in the middle of a contig; missing start; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
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.
 
 0.992
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 
 0.986
leuA-2
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 1 subfamily.
 
 
 0.973
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 1 subfamily.
 
 
 0.963
OME88920.1
Citramalate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.953
OME95247.1
GNAT family N-acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.950
ilvD
Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.
 
 
 0.941
Your Current Organism:
Paenibacillus lautus
NCBI taxonomy Id: 1401
Other names: ATCC 43898, Bacillus lautus, CIP 103118, DSM 3035, IFO 15380, JCM 9073, LMG 11157, LMG:11157, NBRC 15380, NRRL NRS-666, P. lautus, Paenibacillus sp. HF_07
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