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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
tyrBAromatic-amino-acid aminotransferase. (398 aa)    
Predicted Functional Partners:
pheA
Prephenate dehydratase.
    
 0.994
hpd_1
4-hydroxyphenylpyruvate dioxygenase.
  
 
 0.989
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
    
 0.987
phhA
Phenylalanine-4-hydroxylase.
  
 
 0.982
mtnD
Acireductone dioxygenase.
     
 0.968
hisC
Histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
 
 0.963
hisC2
Histidinol-phosphate aminotransferase 2; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
  
 
 0.963
metH
Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
     
 0.962
metK
S-adenosylmethionine synthase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
 
 0.961
msrC
Free methionine-R-sulfoxide reductase.
    
  0.958
Your Current Organism:
Pseudomonas fluorescens
NCBI taxonomy Id: 294
Other names: ATCC 13525, Bacillus fluorescens, Bacillus fluorescens liquefaciens, Bacterium fluorescen, CCEB 546, CFBP 2102, CIP 69.13, DSM 50090, IAM 12022, IFO 14160, JCM 5963, Liquidomonas fluorescens, NBRC 14160, NCCB 76040, NCIB 9046, NCIB:9046, NCIMB 9046, NCTC 10038, NRRL B-14678, P. fluorescens, Pseudomonas sp. AU2390, Pseudomonas sp. BZ64, Pseudomonas sp. FY32, Pseudomonas sp. HSA2/2016, Pseudomonas sp. HSA3/2016, Pseudomonas sp. ISSDS-433, Pseudomonas sp. JCM 17186, Pseudomonas sp. JCM 2779, Pseudomonas sp. KH-20150KS3, Pseudomonas sp. LBUM223, Pseudomonas sp. LBUM636, Pseudomonas sp. SM2/2016, RH 818, VKM B-894, bacterium P1-1, strain M. Rhodes 28/5
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