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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
BF49_187123butanediol dehydrogenase Ralcohol forming R and Sacetoinspecific EC 1114. (359 aa)    
Predicted Functional Partners:
BF49_4033
5aminolevulinate synthase EC 23137.
  
 
 0.729
tal
Transaldolase EC 2212 Glucose6phosphate isomerase EC 5319; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway; Belongs to the GPI family.
  
 
 0.694
BF49_1872
FIG00444197 hypothetical protein.
       0.606
BF49_6971
Hypothetical protein.
  
 
 0.595
BF49_7289
FIG00441112 hypothetical protein.
  
   
 0.587
BF49_0969
Alcohol dehydrogenase.
 
0.548
BF49_1904
Alcohol dehydrogenase EC 1111.
 
0.530
BF49_1416
Aminotransferase class III.
 
 0.528
BF49_3201
Superoxide dismutase Fe EC 11511; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.
   
  
 0.527
guaA
GMP synthase glutaminehydrolyzing EC 6352; Catalyzes the synthesis of GMP from XMP.
    
  0.526
Your Current Organism:
Bradyrhizobium sp.
NCBI taxonomy Id: 376
Other names: B. sp.
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