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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 20928: PQB biosynthetic 3-oxoacyl-[acyl-carrier-protein] ...

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
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.
 13 A0A077JNI1 A0A0C7ACN7 A0A0H2Z7U1 A0A0H3QWQ9 A0A0P1DFH3 A0A157WSK3 A0A1C7BI89 A0A1D5BKS0 A0A1E9CC50 A0A1F0IY07
(3 more...)
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.
 4 A0A077JNI1 A0A0H2Z7U1 A0A157WSK3 W1MPZ0
2-heptyl-4(1H)-quinolone synthase. [EC: 2.3.1.230]
Octanoyl-CoA + 2-aminobenzoylacetate = 2-heptyl-4(1H)-quinolone + CoA + CO(2) + H(2)O.
  • The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex.
  • The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue.
  • Together with the PqsB subunit, the proteins catalyze the coupling of the octanoyl group with 2-aminobenzoylacetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
 1 P20582