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
thrCThreonine synthase. (469 aa)    
Predicted Functional Partners:
hom
Homoserine dehydrogenase.
 
 
 0.994
ilvA-I
Threonine deaminase; 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.
  
 
 0.968
ilvA-II
Threonine deaminase; 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.
  
 
 0.968
PP_2930
Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
 
 
 0.948
serC
Phosphoserine 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.
   
 0.939
PP_3191
Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.
  
 
 0.938
PP_4430
Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
  
 
 0.938
ltaE
Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
  
 0.926
thrB
Homoserine kinase; Function experimentally demonstrated in the studied genus; enzyme; Belongs to the pseudomonas-type ThrB family.
    
 0.915
PP_0662
Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
  
  
 
0.907
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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