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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_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 52353: Probable 3-ketoacyl-CoA synthase 20

There are 5 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
Very-long-chain 3-oxoacyl-CoA synthase. [EC: 2.3.1.199]
A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO(2).
  • This is the first component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs.
  • Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids.
  • For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate, while CER6 from the same plant prefers substrates with chain length of C(22) to C(32).
  • Cf. EC 1.1.1.330, EC 4.2.1.134 and EC 1.3.1.93.
  • Formerly EC 2.3.1.119 and EC 2.3.1.n8.
 27 A0A178UBW3 A0A178UE45 A0A178UUK5 A0A178UZI2 A0A178VRM0 A0A178W124 A0A178W4M1 A0A178WCX7 A0A178WF97 A4VCL7
(17 more...)
Naringenin-chalcone synthase. [EC: 2.3.1.74]
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO(2).
  • In the presence of NADH and a reductase, 6'-deoxychalcone is produced.
 2 A0A0B2PTR2 A0A0B2QML7
Beta-ketoacyl-[acyl-carrier-protein] synthase I. [EC: 2.3.1.41]
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
  • Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain.
  • Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids.
  • Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)).
  • The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
 2 A0A0B2Q8X8 A0A0B2QJJ4
Beta-ketoacyl-[acyl-carrier-protein] synthase III. [EC: 2.3.1.180]
Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO(2).
  • Involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria.
  • In contrast to EC 2.3.1.41 and EC 2.3.1.179, this enzyme specifically uses CoA thioesters rather than acyl-ACP as the primer.
  • In addition to the above reaction, the enzyme can also catalyze the reaction of EC 2.3.1.38, but to a much lesser extent.
  • Responsible for initiating both straight- and branched-chain fatty- acid biosynthesis, with the substrate specificity in an organism reflecting the fatty-acid composition found in that organism.
  • For example, Streptococcus pneumoniae, a Gram-positive bacterium, is able to use both straight- and branched-chain (C4--C6) acyl-CoA primers whereas Escherichia coli, a Gram-negative organism, uses primarily short straight-chain acyl CoAs, with a preference for acetyl-CoA.
 2 A0A0B2Q8X8 A0A0B2QJJ4
Transferred entry: 1.1.1.330, 1.3.1.93, 2.3.1.199 and 4.2.1.134. [EC: 2.3.1.119]
    		1 A0A0D2MBC4