This entry represents a subgroup of thiolase-like domains (missing a few subfamilies). These domains have a 3-layer structure with an alpha/beta/alpha topology. This domain usually occurs in two similar copies that are related by a pseudo-dyad, and which arose through duplication. The proteins in this entry can be split into two groups: those related to thiolase, and those related to chalcone synthase. The thiolase-like enzymes include:

• Thiolase, where the topology of each domain is similar to the first domain of phosphoglucomutase [1]
• Beta-ketoacyl-ACP synthases types I (2.3.1.41) and II (2.3.1.179) [2, 3]
• Actinorhodin polyketide beta-ketoacyl synthases 1 and 2 [4]

The chalcone synthase-like enzymes include:

• Chalcone synthase (2.3.1.74) [5]
• Polyketide synthases [6]
• Dihydropinosylvin synthase [7]

1. The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. J. Mol. Biol. 273, 714-28
2. Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases. FEBS J. 273, 695-710
3. Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. EMBO J. 17, 1183-91
4. An antibiotic factory caught in action. Nat. Struct. Mol. Biol. 11, 888-93
5. Structure-guided programming of polyketide chain-length determination in chalcone synthase. Biochemistry 40, 14829-38
6. A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites. Nat. Struct. Mol. Biol. 11, 894-900
7. An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases. Chem. Biol. 11, 1179-94

This entry represents a subgroup of thiolase-like domains (missing a few subfamilies). These doma
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