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CATH Superfamily 3.30.930.10

Bira Bifunctional Protein; Domain 2

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:

"
Bira Bifunctional Protein; Domain 2
".

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 32550: Lipoate-protein ligase a related

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
Lipoyl(octanoyl) transferase. [EC: 2.3.1.181]
Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
  • The first committed step in the biosynthesis of lipoyl cofactor.
  • The lipoyl cofactor is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein.
  • Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
  • Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate.
  • The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8.
  • An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs).
 1618 A0A023CLX7 A0A023CLX7 A0A023DE05 A0A023DE05 A0A023PBZ6 A0A023PBZ6 A0A033V0J8 A0A033V0J8 A0A060LUU5 A0A060LUU5
(1608 more...)
Transferred entry: 6.3.1.20. [EC: 2.7.7.63]
    		36 A0A075GVJ5 A0A075GVJ5 A0A0A8WBP6 A0A0A8WBP6 A0A0B2ZZJ7 A0A0B2ZZJ7 A0A0B3A6F6 A0A0B3A6F6 A0A0C7QXR3 A0A0C7QXR3
    (26 more...)
    Lipoate--protein ligase. [EC: 6.3.1.20]
    ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl- carrier protein]-N(6)-(lipoyl)lysine + AMP + diphosphate.
    • This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid.
    • The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
    • Lipoylation is essential for the function of these enzymes.
    • The enzyme can also use octanoate instead of lipoate.
    • Formerly EC 2.7.7.63.
    		 18 A6ZPT1 A6ZPT1 B3LQ66 B3LQ66 B5VLD2 B5VLD2 C7GSU4 C7GSU4 C8ZBG9 C8ZBG9
    (8 more...)