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
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[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. (341 aa)    
Predicted Functional Partners:
kbl
2-amino-3-ketobutyrate CoA ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
 0.999
nifJ
Pyruvate-flavodoxin oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.974
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.
   
 
 0.972
ydfG
Malonic semialdehyde reductase; 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.
    
 0.940
thrC
Threonine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.936
ltaA
Threonine aldolase; Low- specificity; catalyzes the formation of acetaldehyde and glycine from L-threonine; acts on L-threonine, L-allo-threonine, L-threo-phenylserine, and L-erythro-phenylserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
  0.936
adhE
Acetaldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
  
 0.773
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.
 
 0.771
fruA
PTS system fructose-specific transporter subunits IIBC; Phosphoenolpyruvate-dependent sugar phosphotransferase system; catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane; IIB is phosphorylated by IIA and then transfers the phosphoryl group to the sugar; IIC forms the translocation channel; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.688
tdcB
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.
   
 
 0.688
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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