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CATH Superfamily 3.40.50.970

Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains

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: 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 194: Thiamine diphosphate dependent-3-acetyloctanal syn...

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
3-acetyloctanal synthase. [EC: 2.2.1.12]
Pyruvate + (E)-oct-2-enal = (S)-3-acetyloctanal + CO(2).
  • The enzyme, characterized from the bacterium Serratia marcescens, participates in the biosynthesis of the antibiotic prodigiosin.
  • The enzyme decarboxylates pyruvate, followed by attack of the resulting two-carbon fragment on (E)-oct-2-enal, resulting in a Stetter reaction.
  • In vitro the enzyme can act on a number of alpha,beta-unsaturated carbonyl compounds, including aldehydes and ketones, and can catalyze both 1-2 and 1-4 carboligations depending on the substrate.
 1 Q5W251