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:
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Co-occurrence
Co-expression
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[Homology]
Score
neuACMP-N,N'-diacetyllegionaminic acid synthase. (253 aa)    
Predicted Functional Partners:
spsE
N,N'-diacetyllegionaminic acid synthase.
 
  
 0.952
BVIR_1971
Capsule polysaccharide biosynthesis protein.
 
  
 0.941
dxs_2
1-deoxy-D-xylulose-5-phosphate synthase.
 
     0.878
BVIR_1974
Hypothetical protein.
 
     0.845
xecE
2-(S)-hydroxypropyl-CoM dehydrogenase.
 
 
   0.822
BVIR_3149
Glycerate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
      0.542
hisF
Imidazole glycerol phosphate synthase subunit HisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
      0.505
capD
UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase.
 
  
 0.425
wcaJ
UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase.
  
  
 0.418
Your Current Organism:
Blastochloris viridis
NCBI taxonomy Id: 1079
Other names: ATCC 19567, B. viridis, CCUG 30818, CCUG 7830, DSM 133, LMG 4321, LMG:4321, NBRC 102659, Rhodopseudomonas viridis, strain G. Drews F
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