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CATH Superfamily 4.10.320.10

E3-binding domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
E3-binding domain
".

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
Dihydrolipoyllysine-residue succinyltransferase. [EC: 2.3.1.61]
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine.
  • A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
 164 A0A026V2Z6 A0A028AFI7 A0A028DMC8 A0A069XRZ4 A0A070F4M0 A0A070SYN3 A0A070UKA2 A0A072ZIZ6 A0A073UGJ5 A0A0A0FBC9
(154 more...)
Dihydrolipoyllysine-residue acetyltransferase. [EC: 2.3.1.12]
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine.
  • A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
 160 A0A026V705 A0A027ZY08 A0A028E956 A0A045INV6 A0A063XB52 A0A069XNM4 A0A070SQ51 A0A0A0F5H4 A0A0A8U7N8 A0A0B0DPM7
(150 more...)
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase. [EC: 2.3.1.168]
2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.
  • A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A.
  • In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
 16 A0A0P7D5Q2 A0A164X9I3 A0A212R9C4 A0A3G2HJN3 A0A454LPY3 G4EU23 L8AJT2 O06159 P09062 P11181
(6 more...)
Site-specific DNA-methyltransferase (adenine-specific). [EC: 2.1.1.72]
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.
  • This is a large group of enzymes, most of which form so-called 'restriction-modification systems', with nucleases that possess similar site specificity (the nucleases are listed as either EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5).
  • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
 2 D6AX99 Q53609