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  Domain Name: Glycosyltransferase_
Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 68
Total Disease Mutations Found: 46
This domain occurred 9 times on human genes (16 proteins).



  CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IK
  CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IP
  GLYCOGEN STORAGE DISEASE 0, LIVER
  GLYCOGEN STORAGE DISEASE 0, MUSCLE
  GLYCOGEN STORAGE DISEASE VI
  MCARDLE DISEASE


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


No Conserved Features/Sites Found for Glycosyltransferase_


























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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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