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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_3_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 35: Putative lipoyltransferase 2, mitochondrial

There are 1 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).
 106 A0A045HB18 A0A045HB18 A0A045HB18 A0A045HB18 A0A045HB18 A0A045HB18 A0A045HB18 A0A045HB18 A0A0H3LAZ4 A0A0H3LAZ4
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