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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 12462: Type I polyketide synthase

There are 15 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
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.
 70 A0A063BLL2 A0A099KPM6 A0A0D5M5S0 A0A0E0U920 A0A0E2WXI9 A0A0H2ZTV9 A8LFZ9 B2IYN1 B2IYN9 B2IYP7
(60 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.
 24 A0A060Q8N5 A0A0A1VUG9 A0A0K3BQV0 A0A0K3BQV0 A0A1L7MIS0 D0LQX8 G5J2D4 L1KT20 L1KT20 M9TYC9
(14 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.
 15 A0R737 C6WN16 D3D0C0 D5UX42 D6ZB46 E8WEN9 G0PRM1 G0PRM1 G0PRM1 G0PRM4
(5 more...)
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.
 8 A0A063BLL2 A0A0D5M5S0 A0A0E0U920 G0Q9U2 G7LSJ3 G9AAV1 Q39J94 Q5EGQ8
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.
 6 A0A1J0IUB9 A0A1K6ZWD7 U5X0R8 X7T5G5 X7ZBG2 X8CSB1
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.
 6 D4HVB7 E5B1B4 G0PRM3 G0PRM3 Q0RTS3 Q0RTS4
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.
 4 B2IYP7 G0PRM6 G0PRM6 K0JX88
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 2 F9DZB8 G2E5C9
    Ornithine racemase. [EC: 5.1.1.12]
    L-ornithine = D-ornithine.
      		 2 A0A099KPM6 I9NJT0
      Narbonolide synthase. [EC: 2.3.1.240]
      Malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH = narbonolide + 7 CoA + 7 CO(2) + 5 NADP(+) + 2 H(2)O.
      • The product, narbonolide, contains a 14-membered ring and is an intermediate in the biosynthesis of narbonomycin and pikromycin in the bacterium Streptomyces venezuelae.
      • The enzyme also produces 10-deoxymethynolide (see EC 2.3.1.239).
      • The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain.
      • Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP).
      • Not all active sites are used in the biosynthesis.
      		 2 Q9ZGI3 Q9ZGI5
      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 Q54FI3 Q55E72
      [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.
      		 2 G0PUE4 G0Q9U9
      Enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific). [EC: 1.3.1.10]
      An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADPH.
      • One of the activities of EC 2.3.1.86, an enzyme found in yeasts (Ascomycota and the Basidiomycota).
      • Catalyzes the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16.
      • The yeast enzyme is Si-specific with respect to NADP(+).
      • Cf. EC 1.3.1.39 and EC 1.3.1.104 which describes enzymes whose stereo-specificity toward NADPH is not known.
      • See also EC 1.3.1.9.
      		 2 Q0RIF6 Q0RIF6
      10-deoxymethynolide syntase. [EC: 2.3.1.239]
      Malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH = 10-deoxymethynolide + 6 CoA + 6 CO(2) + 5 NADP(+) + 2 H(2)O.
      • The product, 10-deoxymethynolide, contains a 12-membered ring and is an intermediate in the biosynthesis of methymycin in the bacterium Streptomyces venezuelae.
      • The enzyme also produces narbonolide (see EC 2.3.1.240).
      • The enzyme has 29 active sites arranged in four polypeptides (pikAI - pikAIV) with a loading domain, six extension modules and a terminal thioesterase domain.
      • Each extension module contains a ketosynthase (KS), keto reductase (KR), an acyltransferase (AT) and an acyl-carrier protein (ACP).
      • Not all active sites are used in the biosynthesis.
      		 2 Q9ZGI3 Q9ZGI5
      Glutamate racemase. [EC: 5.1.1.3]
      L-glutamate = D-glutamate.
        		 1 I8U1X2
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