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
ilvHAcetolactate synthase III, thiamin-dependent, small subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (158 aa)    
Predicted Functional Partners:
ilvI
Acetolactate synthase III, large subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 
 0.999
ilvC
Acetohydroxy acid isomeroreductase and 2-dehydropantoate 2-reductase; 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.
 
 
 0.998
alsS
Acetolactate synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the TPP enzyme family.
 
 0.989
ilvA
L-threonine dehydratase biosynthetic IlvA; 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.
  
 
 0.975
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.
 
 0.974
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.
 
 
 0.966
nifJ
Pyruvate-flavodoxin oxidoreductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 
 0.939
aldB
Alpha-acetolactate decarboxylase; Function experimentally demonstrated in the studied genus; enzyme; Belongs to the alpha-acetolactate decarboxylase family.
     
 0.915
pfl
Formate C-acetyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
     
  0.900
ilvD
Dihydroxyacid dehydratase (ilvD-like); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the IlvD/Edd family.
 
 
 0.837
Your Current Organism:
Lactococcus piscium
NCBI taxonomy Id: 1364
Other names: ATCC 700018, CCUG 32207, CCUG 32732, CIP 104371, DSM 6634, JCM 11055, L. piscium, NCFB 2778, NCIMB 13196, strain HRIA 68
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.