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
KRC23773.1Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. (476 aa)    
Predicted Functional Partners:
KRC24026.1
Homoserine dehydrogenase; Catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.989
KRC26890.1
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.
  
 
 0.978
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.
  
 
 0.976
KRC18416.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.976
KRC23539.1
Threonine dehydratase; Catalyzes the formation of 2-oxobutanoate from L-threonine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.969
thrB
Homoserine kinase; Catalyzes the formation of O-phospho-L-homoserine from L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pseudomonas-type ThrB family.
    
 0.966
serC
3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.958
KRC27062.1
Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.952
KRC27765.1
Threonine aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.927
KRC30655.1
Aspartate kinase; Catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP, in Bacillus, lysine sensitive; regulated by response to starvation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family.
  
 
 0.913
Your Current Organism:
Acidovorax sp. Root217
NCBI taxonomy Id: 1736492
Other names: A. sp. Root217
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