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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 97302: Glycosyltransferase 1 domain-containing protein 1

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
Alpha,alpha-trehalose synthase. [EC: 2.4.1.245]
NDP-alpha-D-glucose + D-glucose = alpha,alpha-trehalose + NDP.
  • The enzyme-catalyzed reaction is reversible.
  • In the reverse direction to that shown above, the enzyme is specific for alpha,alpha-trehalose as substrate, as it cannot use alpha- or beta-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose.
  • While the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-alpha-D-glucose to the same extent, that from the hyperthermophilic archaeon Thermococcus litoralis has a marked preference for ADP-alpha-D-glucose and that from the hyperthermophilic archaeon Thermoproteus tenax has a marked preference for UDP-alpha-D-glucose.
  • Formerly EC 2.4.1.n1.
 14 A0A0S1XEU2 A0A0S1XEU2 I6V3X2 I6V3X2 N1JRJ5 N1JRJ5 O58762 O58762 Q1ARU5 Q1ARU5
(4 more...)
Alpha,alpha-trehalose phosphorylase (configuration-retaining). [EC: 2.4.1.231]
Alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate.
  • Unlike EC 2.4.1.64, this enzyme retains its anomeric configuration.
  • Vanadate is a strong competitive inhibitor of this reversible reaction.
 2 O75003 O75003