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 (O-phospho-L-homoserine phosphate-lyase (adding water;L-threonine-forming)); O-Phospho-L-homoserine + H2O <=> L-Threonine + Orthophosphate / O-Phospho-4-hydroxy-L-threonine + H2O <=> 4-Hydroxy-L-threonine + Orthophosphate. (480 aa)    
Predicted Functional Partners:
thrA/hom
L-Homoserine + NAD+ <=> L-Aspartate 4-semialdehyde + NADH + H+ and L-Homoserine + NADP+ <=> L-Aspartate 4-semialdehyde + NADPH + H+.
 
 
 0.981
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.
  
 
 0.971
serC
Phosphoserine aminotransferase (phosphoserine transaminase); Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine.
   
 0.934
serB/thrH
Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; O-Phospho-L-serine + H2O <=> L-Serine + Orthophosphate and D-O-Phosphoserine + H2O <=> D-Serine + Orthophosphate.
   
 0.930
ask
Aspartokinase (Aspartate kinase); ATP + L-Aspartate <=> ADP + 4-Phospho-L-aspartate; Belongs to the aspartokinase family.
  
 
 0.843
leuD
3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
  
  
 0.809
asd
Aspartate-semialdehyde dehydrogenase (Semialdehyde dehydrogenase); Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
  
 
 0.719
gltB
Glutamate synthase large subunit (Ferredoxin); 2 L-Glutamate + 2 Oxidized ferredoxin <=> L-Glutamine + 2-Oxoglutarate + 2 Reduced ferredoxin.
  
  
 0.708
ilvC
Ketol-acid reductoisomerase (NADP(+)); Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
  
  
 0.668
pdxS
Pyridoxal biosynthesis lyase pdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
   
  
 0.618
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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