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. (343 aa)    
Predicted Functional Partners:
kbl
2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
 
 
 0.988
ilvA
Threonine ammonia-lyase, biosynthetic, long form; 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.
   
 0.908
AFC86773.1
Threonine aldolase; PFAM: Beta-eliminating lyase.
     
 0.901
AFC87517.1
Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase.
     
 0.901
AFC86816.1
Short-chain alcohol dehydrogenase; PFAM: short chain dehydrogenase; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
    
  0.900
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.
 
  
 0.619
AFC87165.1
Polyketide synthase family protein; PFAM: Acyl transferase domain; Phosphopantetheine attachment site; KR domain; Alcohol dehydrogenase GroES-like domain; Beta-ketoacyl synthase, N-terminal domain; Zinc-binding dehydrogenase; Beta-ketoacyl synthase, C-terminal domain.
  
  
 0.584
AFC87167.1
7-keto-8-aminopelargonate synthetase-like enzyme; PFAM: Aminotransferase class I and II; TIGRFAM: 8-amino-7-oxononanoate synthase.
 
  
 0.571
AFC87300.1
Phosphoenolpyruvate-protein phosphotransferase; PFAM: PEP-utilising enzyme, TIM barrel domain; PEP-utilising enzyme, mobile domain; PTS HPr component phosphorylation site; Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; PEP-utilising enzyme, N-terminal; TIGRFAM: Phosphotransferase System HPr (HPr) Family; phosphoenolpyruvate-protein phosphotransferase; Belongs to the PEP-utilizing enzyme family.
     
 0.570
miaA
tRNA isopentenyltransferase MiaA; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family.
  
  
 0.532
Your Current Organism:
Frateuria aurantia
NCBI taxonomy Id: 767434
Other names: F. aurantia DSM 6220, Frateuria aurantia DSM 6220, Frateuria aurantia IFO 3245, Frateuria aurantia str. DSM 6220, Frateuria aurantia strain DSM 6220
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.