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CATH Superfamily 3.40.366.10

Malonyl-Coenzyme A Acyl Carrier Protein, domain 2

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 named:

"
Malonyl-Coenzyme A Acyl Carrier Protein, domain 2
".

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 12448: Polyketide synthase peptide synthetase

There are 9 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
Lovastatin nonaketide synthase. [EC: 2.3.1.161]
9 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO(2) + 11 NADP(+) + S-adenosyl-L-homocysteine + 6 H(2)O.
  • This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase.
  • The PKS catalyzes many of the chain building reactions of EC 2.3.1.85, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
 23 A0A084GE65 B8M0G9 B8M2A8 B8M7V1 B8M9X6 B8MEK8 B8MEL0 B8MFT5 B8MJ47 B8MKY6
(13 more...)
6-deoxyerythronolide-B synthase. [EC: 2.3.1.94]
Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO(2) + H(2)O + 6 NADP(+).
  • The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics.
  • Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3.
  • The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain.
  • Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP).
  • The KS domain both accepts the growing polyketide chain from the previous module and catalyzes the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain.
  • This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms.
 3 A0A084GE65 B8MCM5 B8MM93
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 1 B8MPC7
    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 A0A084GE65
    Enoyl-[acyl-carrier-protein] reductase (NADH). [EC: 1.3.1.9]
    An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.
    • The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety.
    • The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18.
    • The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
    		 1 A5AC09
    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 B8M2A8
    Acetolactate synthase. [EC: 2.2.1.6]
    2 pyruvate = 2-acetolactate + CO(2).
    • The reaction shown is in the pathway of biosynthesis of valine.
    • The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
    • Formerly EC 4.1.3.18.
    		 1 A0A0A2V1Z9
    2-methylbutanoate polyketide synthase. [EC: 2.3.1.244]
    2 malonyl-CoA + [2-methylbutanoate polyketide synthase] + 2 NADPH + S-adenosyl-L-methionine = (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] + 2 CoA + 2 CO(2) + 2 NADP(+) + S-adenosyl-L- homocysteine + H(2)O.
    • This polyketide synthase enzyme forms the (S)-2-methylbutanoate side chain during lovastatin biosynthesis by the filamentous fungus Aspergillus terreus.
    • The overall reaction comprises a single condensation reaction followed by alpha-methylation, beta-ketoreduction, dehydration, and alpha,beta enoyl reduction.
    		 1 Q3S2U6
    6-methylsalicylic acid synthase. [EC: 2.3.1.165]
    Acetyl-CoA + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 4 CoA + 3 CO(2) + NADP(+).
    • A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein.
    • It has a similar sequence to vertebrate type I fatty acid synthase.
    • Acetoacetyl-CoA can also act as a starter molecule.
    		 1 A0A084GE65