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: waiting to be named.

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 11510: 2-oxoisovalerate dehydrogenase, beta subunit

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
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring). [EC: 1.2.4.4]
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine- residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2).
  • It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2- oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine.
  • It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
  • Formerly EC 1.2.4.3.
89 A0A031FP07 A0A067A5E4 A0A072ZNM6 A0A083UKZ0 A0A0A1HVV8 A0A0A4HUR2 A0A0A6FFC0 A0A0A7PQH0 A0A0B7D9Z7 A0A0C2A8J5
(79 more...)
Pyruvate dehydrogenase (acetyl-transferring). [EC: 1.2.4.1]
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
  • It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
3 A0A0Q6YPB4 G8QBA9 Q1I713
2-oxoisovalerate dehydrogenase (acylating). [EC: 1.2.1.25]
3-methyl-2-oxobutanoate + CoA + NAD(+) = 2-methylpropanoyl-CoA + CO(2) + NADH.
  • Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2- oxopentanoate.
1 Q88EQ1