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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
OPJ55315.1Glycosyl transferases group 1. (305 aa)    
Predicted Functional Partners:
glgB
1,4-alpha-glucan branching enzyme GlgB; Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position; Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
   
 0.922
OPJ55312.1
Polysaccharide biosynthesis protein.
  
 
 0.898
OPJ55316.1
O-antigen ligase.
  
 
 0.887
pglC
Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase.
  
 
 0.842
lnpD
UDP-glucose 4-epimerase; Belongs to the NAD(P)-dependent epimerase/dehydratase family.
    
 0.815
glgP
Glycogen phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
  
 0.786
epsH
Putative glycosyltransferase EpsH.
  
 
 0.778
epsD
Putative glycosyltransferase EpsD.
       0.773
OPJ56215.1
Fibronectin type III domain protein.
  
     0.768
epsN
Putative pyridoxal phosphate-dependent aminotransferase EpsN; Belongs to the DegT/DnrJ/EryC1 family.
  
 
 0.749
Your Current Organism:
Clostridium thermoalcaliphilum
NCBI taxonomy Id: 29349
Other names: ATCC 51508, CIP 105528, DSM 7309, [. thermoalcaliphilum, [Clostridium] thermoalcaliphilum, strain JW/YL23-2
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