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
KRC27765.1Threonine aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (355 aa)    
Predicted Functional Partners:
gcvP
Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
    
 0.953
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
   
 0.936
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.
     
 0.934
KRC23773.1
Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.927
KRC23539.1
Threonine dehydratase; Catalyzes the formation of 2-oxobutanoate from L-threonine; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.899
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.
     
 0.899
KRC18416.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.899
KRC23691.1
FAD-dependent oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.860
KRC28170.1
Class V aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.860
KRC12652.1
Serine--glyoxylate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.792
Your Current Organism:
Acidovorax sp. Root217
NCBI taxonomy Id: 1736492
Other names: A. sp. Root217
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