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CATH Superfamily 3.40.47.10

Thiolase/Chalcone synthase

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_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.

Superfamily: Thiolase/Chalcone synthase

This superfamily entry comprises structural domains found in enzymes related to thiolase and chalcone synthase. It has a 3-layer alpha/beta/alpha topology and usually occurs in two similar copies that are related by a pseudo-dyad, and which arose through duplication.

The domain can be found in thiolase and homologous enzymes including: beta-ketoacyl-acyl carrier protein (ACP) synthases (types I and II) PMID:16441657,PMID:9482715, actinorhodin polyketide beta-ketoacyl synthases 1 and 2 PMID:15286722, fatty oxidation complex beta subunit (3-ketoacyl-CoA thiolase) PMID:9402066, as well as in chalcone synthase PMID:11732902 and homologous enzymes such as: ketoacyl-ACP synthase III (FabH) PMID:11243824, polyketide synthases PMID:15286723, 3-hydroxy-3-methylglutaryl CoA synthase PMID:15292254, dihydropinosylvin synthase PMID:15380179.

INTERPRO:IPR016039,

GO Diversity

Unique GO annotations
399 Unique GO terms

EC Diversity

Unique EC annotations
55 Unique EC terms

Species Diversity

Unique species annotations
21919 Unique species

Sequence/Structure Diversity

Overview of the sequence / structure diversity of this superfamily compared to other superfamilies in CATH. Click on the chart to view the data in more detail.

Superfamily Summary

A general summary of information for this superfamily.
Structures
Domains: 2188
Domain clusters (>95% seq id): 275
Domain clusters (>35% seq id): 79
Unique PDBs: 446
Alignments
Structural Clusters (5A): 11
Structural Clusters (9A): 8
FunFam Clusters: 310
Function
Unique EC: 55
Unique GO: 399
Taxonomy
Unique Species: 21919
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