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
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. (342 aa)    
Predicted Functional Partners:
kbl
2-amino-3-ketobutyrate CoA ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
 0.996
Psdht
Pyridoxal-5'-phosphate-dependent protein subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.910
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.
   
 0.910
ThrC
Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.903
YdfG
NAD(P)-dependent oxidoreductase; NADP(+)-dependent; catalyzes the formation of 3-hydroxypropionate from the toxic malonic semialdehyde, catalyzes the formation of 2-aminomalonate-semialdehyde from L-serine; can also use 3-hydroxybutyrate, 3-hydroxy-isobutyrate, D-threonine, L-allo-threonine,D-serine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
    
 0.902
bioF
8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
  
 0.632
AOI81616.1
8-amino-7-oxononanoate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.630
rplU
50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
      
 0.545
puuR_4
DNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.518
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.