STRINGSTRING
PBAL39_21810 protein (Pedobacter sp. BAL39) - STRING interaction network
"PBAL39_21810" - L-allo-threonine aldolase in Pedobacter sp. BAL39
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PBAL39_21810L-allo-threonine aldolase (340 aa)    
Predicted Functional Partners:
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 (423 aa)
     
  0.911
gcvP
Glycine dehydrogenase (aminomethyl-transferring) ; 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 (959 aa)
       
  0.904
ilvA
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 (416 aa)
     
 
  0.870
PBAL39_04673
Threonine synthase (436 aa)
     
    0.862
PBAL39_06231
Folylpolyglutamate synthase (412 aa)
       
    0.856
PBAL39_21960
2-amino-3-ketobutyrate CoA ligase (Glycine acetyltransferase) (413 aa)
   
 
  0.853
kbl
Glycine acetyltransferase ; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA (395 aa)
   
 
  0.852
PBAL39_01842
Aldehyde-alcohol dehydrogenase (876 aa)
   
 
  0.848
PBAL39_02332
8-amino-7-oxononanoate synthase (401 aa)
   
 
  0.840
PBAL39_04658
Methionine synthase (1219 aa)
       
    0.840
Your Current Organism:
Pedobacter sp. BAL39
NCBI taxonomy Id: 391596
Other names: P. sp. BAL39, Pedobacter BAL39, Pedobacter sp. BAL39
Server load: low (6%) [HD]