CATH Classification
Domain Context
CATH Clusters
| Superfamily | Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A | 
| Functional Family | Glycogenin-1 isoform 1 | 
Enzyme Information
| 2.4.1.186 | 
							 Glycogenin glucosyltransferase. 
							based on mapping to UniProt P46976 		
							UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin. 
							-!- The first reaction of this enzyme is to catalyze its own glucosylation, normally at a specific Tyr of the protein if this group is free; when the Tyr is replaced by Thr or Phe, the enzyme's self-glucosylation activity is lost but its intermolecular transglucosylation ability remains. -!- It continues to glucosylate an existing glucosyl group until a length of about 5-13 residues has been formed. -!- Further lengthening of the glycogen chain is then carried out by EC 2.4.1.11. -!- Not highly specific for the donor, using UDP-xylose in addition to UDP-glucose (although not glucosylating or xylosylating a xylosyl group so added). -!- It can also use CDP-glucose and TDP-glucose, but not ADP-glucose or GDP-glucose. -!- Similarly it is not highly specific for the acceptor, using water (i.e. hydrolyzing UDP-glucose) among others. -!- Various forms of the enzyme exist, and different forms predominate in different organs. -!- Thus primate liver contains glycogenin-2, of molecular mass 66 kDa, whereas the more widespread form is glycogenin-1, with a molecular mass of 38 kDa. -!- Formerly EC 2.4.1.112. 
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UniProtKB Entries (1)
| P46976 | 
						 GLYG_HUMAN 
						Homo sapiens 
						Glycogenin-1 
					 | 
				
PDB Structure
| PDB | 3U2V | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | 
					 Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis. 
					    
					    Proc.Natl.Acad.Sci.USA 
					    
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