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feaB feaB tynA tynA feaR feaR paaK paaK paaI paaI fmt fmt paaJ paaJ pheA pheA tyrB tyrB yahK yahK tyrA tyrA
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query proteins and first shell of interactors
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second shell of interactors
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Predicted Interactions
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textmining
co-expression
protein homology
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feaBPhenylacetaldehyde dehydrogenase; Acts almost equally well on phenylacetaldehyde, 4- hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde. (499 aa)    
Predicted Functional Partners:
tynA
Tyramine oxidase, copper-requiring; The enzyme prefers aromatic over aliphatic amines; Belongs to the copper/topaquinone oxidase family.
 
 
 0.992
feaR
Transcriptional activator for tynA and feaB; Positive regulator of tynA/maoA and feaB/padA, the genes for 2-phenylethylamine catabolism.
  
  
 0.959
paaK
phenylacetyl-CoA ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
  
 0.942
paaI
hydroxyphenylacetyl-CoA thioesterase; Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3- hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA. Belongs to the thioesterase PaaI family.
  
 
  0.907
fmt
10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Belongs to the Fmt family.
 
      0.886
paaJ
3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase; Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA. Belongs to the thiolase-like superfamily. Thiolase family.
   
 
 0.736
pheA
Chorismate mutase and prephenate dehydratase, P-protein; Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
      
 0.693
tyrB
Tyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
   
 
 0.687
yahK
Broad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined. Belongs to the zinc-containing alcohol dehydrogenase family.
  
  
 0.631
tyrA
Chorismate mutase-T and prephenate dehydrogenase; Protein involved in L-phenylalanine biosynthetic process and tyrosine biosynthetic process.
      
 0.605
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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