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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
tdhL-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. (344 aa)    
Predicted Functional Partners:
kbl-2
2-amino-3-ketobutyrate CoA ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
 
 0.993
kbl
2-amino-3-ketobutyrate CoA ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
 
 0.983
AMS41455.1
Serine dehydratase; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
   
 0.914
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.
   
 0.914
AMS43730.1
Pfam:pfam14821 Threonine synthase N terminus.
   
 
 0.905
AMS43989.1
Threonine synthase-like protein; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
   
 
 0.905
AMS40946.1
Hypothetical protein; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.
    
 0.903
AMS39548.1
L-threonine 3-dehydrogenase; Pfam:pfam08240 Alcohol dehydrogenase GroES-like domain.
  
  
 
0.902
AMS39595.1
2-amino-3-ketobutyrate coenzyme A ligase; Pfam:pfam00155 Aminotransferase class I and II.
 
  
 0.565
AMS43322.1
Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.
  
 
 0.564
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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