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
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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
KGM29936.1Endoribonuclease L-PSP; Derived by automated computational analysis using gene prediction method: Protein Homology. (114 aa)    
Predicted Functional Partners:
KGM29935.1
ATP-dependent helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.545
pheA
Chorismate mutase; Catalyzing the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.489
KGM28815.1
Serine dehydratase; Catalyzes the formation of 2-oxobutanoate from L-threonine or the formation of pyruvate from serine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.462
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.
  
 0.462
dadA
Amino acid dehydrogenase; Oxidative deamination of D-amino acids.
 
  
 0.414
Your Current Organism:
Photorhabdus luminescens
NCBI taxonomy Id: 29488
Other names: ATCC 29999, CIP 106429, DSM 3368, P. luminescens, Xenorhabdus luminescens, strain Hb
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