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CATH Superfamily 2.130.10.10

YVTN repeat-like/Quinoprotein amine dehydrogenase

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:

"
YVTN repeat-like/Quinoprotein amine dehydrogenase
".

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 102838: E3 ubiquitin-protein ligase COP1

There are 3 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
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 18 A0A0B2NS72 A0A0B2PAQ2 A0A0B2Q7D9 A0A0B2QAG1 A0A0B2QVK0 A0A0B2QWI5 A0A0B2R8D1 A0A0B2RTB6 A0A0B2RXA1 A0A0B2SKF0
(8 more...)
Transferred entry: 2.3.2.23, 2.3.2.27 and 6.2.1.45. [EC: 6.3.2.19]
    		14 A0A0B2NS72 A0A0B2PAQ2 A0A0B2Q7D9 A0A0B2QAG1 A0A0B2QVK0 A0A0B2QWI5 A0A0B2R8D1 A0A0B2RTB6 A0A0B2RXA1 A0A0B2S2X0
    (4 more...)
    RING-type E3 ubiquitin transferase. [EC: 2.3.2.27]
    S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
    • The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein.
    • The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26).
    • RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
    • Formerly EC 6.3.2.19 and EC 6.3.2.21.
    		 7 A0A178VXE2 H2R8E1 P43254 P93471 Q546Q0 Q8NHY2 Q9R1A8