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CATH Superfamily 3.40.50.2000

Glycogen Phosphorylase B;

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Glycogen Phosphorylase B;
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 26571: Glycosyltransferase WbpY

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Glycogen(starch) synthase. [EC: 2.4.1.11]
UDP-alpha-D-glucose + ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha- D-glucosyl)(n+1).
  • The description (official name) varies according to the source of the enzyme and the nature of its synthetic product.
  • Glycogen synthase from animal tissues is a complex of a catalytic subunit and the protein glycogenin.
  • The enzyme requires glucosylated glycogenin as a primer; this is the reaction product of EC 2.4.1.186.
  • A similar enzyme utilizes ADP-glucose (cf. EC 2.4.1.21).
 13 A0A069PXN4 A0A0C7AQZ2 A0A0E1B3V3 A0A0H2ZJB5 A0A0H3QND5 A0A0P1DIF9 A0A157VM14 A0A1D5BPA7 A0A1E9CAN1 A0A1F0ISP1
(3 more...)
D-inositol-3-phosphate glycosyltransferase. [EC: 2.4.1.250]
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = UDP + 1-O- (2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate.
  • The enzyme, which belongs to the GT-B fold superfamily, catalyzes the first dedicated reaction in the biosynthesis of mycothiol.
  • The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate.
  • A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate.
  • Formerly EC 2.4.1.n3.
 10 A0A0C7AQZ2 A0A0E1B3V3 A0A0H2ZJB5 A0A0H3QND5 A0A157VM14 A0A1D5BPA7 A0A1E9CAN1 A0A1F0ISP1 A0A1G5LS72 Q9HTB9
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