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CATH Superfamily 3.10.110.10

Ubiquitin Conjugating Enzyme

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:

"
Ubiquitin Conjugating Enzyme
".

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 6045: Ubiquitin-conjugating enzyme E2 G1

There are 4 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
Transferred entry: 2.3.2.23, 2.3.2.27 and 6.2.1.45. [EC: 6.3.2.19]
    		91 A0A024V6G7 A0A024WQW0 A0A024X9B2 A0A060RXF3 A0A074T438 A0A075B1D2 A0A075B329 A0A086JZW8 A0A086KNH4 A0A086LAL3
    (81 more...)
    E2 ubiquitin-conjugating enzyme. [EC: 2.3.2.23]
    S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine.
    • The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself.
    • In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
    • Formerly EC 6.3.2.19.
    		 72 A0A096NID2 A0A096P2F5 A0A0A1DXV4 A0A0D9RL78 A0A0L8VKT9 A0A0L8VSU3 A0A0P6J3F6 A0A178V960 A0A1D5Q1Z4 A2VE20
    (62 more...)
    Glucose-6-phosphate isomerase. [EC: 5.3.1.9]
    D-glucose 6-phosphate = D-fructose 6-phosphate.
    • Also catalyzes the anomerization of D-glucose 6-phosphate.
    		 1 A0A0B1TJ19
    Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
    [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
    • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
    • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
    		 1 A0A0E9NKS1