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aroE protein (Thermoproteus tenax) - STRING interaction network
"aroE" - Shikimate 5-dehydrogenase in Thermoproteus tenax
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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aroEShikimate 5-dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA) (266 aa)    
Predicted Functional Partners:
aroD
3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3- dehydroshikimate (297 aa)
  0.999
aroK
Shikimate kinase (272 aa)
 
   
  0.997
aroB
3-dehydroquinate synthase (342 aa)
 
  0.994
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system (364 aa)
 
  0.983
aroA
3-phosphoshikimate 1-carboxyvinyltransferase (404 aa)
 
  0.979
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (432 aa)
   
 
  0.893
alaS
Alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (893 aa)
   
 
  0.851
pfp
Pyrophosphate-dependent phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions (337 aa)
   
      0.838
trpE
Anthranilate synthase component I (419 aa)
 
 
  0.836
exsB
exsB family regulator, ATPase and glucosamine 6-phosphate synthetase domains (484 aa)
     
 
  0.795
Your Current Organism:
Thermoproteus tenax
NCBI taxonomy Id: 768679
Other names: T. tenax, T. tenax Kra 1, Thermoproteus tenax, Thermoproteus tenax DSM 2078, Thermoproteus tenax JCM 9277, Thermoproteus tenax Kra 1, Thermoproteus tenax str. Kra 1, Thermoproteus tenax strain Kra 1
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