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CATH Superfamily 3.30.559.10

Chloramphenicol acetyltransferase-like domain

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:

"
Chloramphenicol acetyltransferase-like 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.
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FunFam 22026: 2-oxoglutarate dehydrogenase E2 component

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
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.
 85 A0A0T9YPK6 A0A0T9ZLK7 A0A0U0RSR4 A0A0U0T2D8 A0A0U0XSZ9 A0A0U1BY60 A0A1M8GUB1 A0A1M8KX94 A0A1M8MD71 A0A1M8U818
(75 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.
 15 A0A045INV6 A0A083W328 A0A0G4E3L1 A0A0H3LBY1 A0A109SPJ1 A0A197IVK9 A5U4P3 F8M0M4 I6XDT2 M8CLH6
(5 more...)
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