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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 52631: Polyketide synthase of type I

There are 6 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 II. [EC: 2.3.1.179]
(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier- protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
  • Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria.
  • While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme.
  • The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature.
  • Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures.
 2 A0A080URI7 A0A0H3E374
Phenylalanine--tRNA ligase. [EC: 6.1.1.20]
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe).
    		 1 G4EW23
    [Acyl-carrier-protein] S-acetyltransferase. [EC: 2.3.1.38]
    Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier- protein].
    • Essential, along with EC 2.3.1.39, for the initiation of fatty-acid biosynthesis in bacteria.
    • The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide.
    • This is one of the activities associated with EC 2.3.1.180.
    		 1 I2C5E7
    Long-chain-fatty-acid--CoA ligase. [EC: 6.2.1.3]
    ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
    • Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity.
    • The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24).
    		 1 A0A150KYP0
    N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase. [EC: 6.3.2.26]
    L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H(2)O = N-(L-5- amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate.
    • The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction.
    • Forms part of the penicillin biosynthesis pathway.
    		 1 I2C5E7
    Mycocerosate synthase. [EC: 2.3.1.111]
    (1) A long-chain acyl-CoA + 3 methylmalonyl-CoA + 6 NADPH + a holo- [mycocerosate synthase] = a trimethylated-mycocerosoyl-[mycocerosate synthase] + 4 CoA + 3 CO(2) + 6 NADP(+) + 3 H(2)O. (2) A long-chain acyl-CoA + 4 methylmalonyl-CoA + 8 NADPH + a holo- [mycocerosate synthase] synthase = a tetramethylated-mycocerosoyl- [mycocerosate synthase] + 5 CoA + 4 CO(2) + 8 NADP(+) + 4 H(2)O.
    • This mycobacterial enzyme loads long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8- tetramethyloctacosanoate (C(32)-mycocerosate).
    • Since the enzyme lacks a thioesterase domain, the products remain bound to the enzyme and require additional enzyme(s) for removal.
    • Even though the enzyme can accept C(6) to C(20) substrates in vitro, it prefers to act on C(14)-C(20) substrates in vivo.
    		 1 A5G645