Conserved Protein Domain Family
Glycosyltransferase_GTB_type

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cl10013: Glycosyltransferase_GTB_type Superfamily (this model, PSSM-Id:299143 is obsolete and has been replaced by 471961)
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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.
Links
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Taxonomy: root
PubMed: 118 links
Protein: Related Protein
Related Structure
Statistics
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Accession: cl10013
PSSM Id: 299143
Name: Glycosyltransferase_GTB_type
Created: 6-Oct-2008
Updated: 2-Feb-2016
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