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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 12512: Polyketide synthase type I

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
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.
 85 A0A045HMI5 A0A0E7SSY2 A0A0E8TZ49 A0A0E8W4G6 A0A0H3L9K2 A0A0H3LC87 A0A0H3M6L3 A0A0H3M8C2 A0A0H3P2W5 A0A0H5J2L2
(75 more...)
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.
 37 A0A0E8V6Y3 A0A0H3A006 A0A0H3LD93 A0A0H3MGR2 A0A0T9CTW6 A0A0U0WZ95 A0A197IW16 A0A1A9EB00 A0A1K2RK53 A0A1K2T1E3
(27 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.
 25 A0A011N152 A0A011QU70 A0A0E2WXI9 A0A0H2ZTV9 A0A0H4W8M6 A0A0J6C4P8 A0A0M7DIF5 A8L4A9 D0LQX2 D0LQX5
(15 more...)
[Acyl-carrier-protein] S-malonyltransferase. [EC: 2.3.1.39]
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].
  • Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria.
  • Also provides the malonyl groups for polyketide biosynthesis.
  • The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis.
  • In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate.
  • This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89.
  • Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase.
  • In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates.
  • The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
 15 A0A0A1FS78 A0A0K3AYS9 A0A0K3BMP5 A0A0K3BQ68 A0A1L7MDJ3 A0A1L7MIS0 A0A1M4EE76 D0LQX8 K0VB34 M9TYD5
(5 more...)
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.
 7 A0A135LPW2 A0A1L7ESK6 A0A1L7F9W4 A1CFL8 K0K2V5 P22367 Q0CJ59
NADPH:quinone reductase. [EC: 1.6.5.5]
NADPH + 2 quinone = NADP(+) + 2 semiquinone.
  • Specific for NADPH.
  • Catalyzes the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates.
  • Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhibitors with respect to the quinone substrate.
  • The semiquinone free-radical product may be non-enzymically reduced to the hydroquinone or oxidized back to quinone in the presence of O(2).
  • Abundant in the lens of the eye of some mammalian species.
 2 W6VVA8 W6WTW1
Ornithine racemase. [EC: 5.1.1.12]
L-ornithine = D-ornithine.
    		 1 G0Q416
    3-oxoacyl-[acyl-carrier-protein] reductase. [EC: 1.1.1.100]
    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH.
    • Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.
    		 1 D0LQX5
    [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 G0PUE4