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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 12565: Polyketide synthase type I

There are 24 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.
 199 A0A031HMT8 A0A068QUF5 A0A068QUF5 A0A073C9W9 A0A073CFT1 A0A073CT05 A0A077N6C5 A0A077N6C5 A0A077NGC4 A0A077NGC4
(189 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.
 100 A0A074TKW5 A0A086JT20 A0A086JT50 A0A086JYV0 A0A086JYW5 A0A086KQG0 A0A086KQL2 A0A086LSF6 A0A086LSF6 A0A086PSR3
(90 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.
 90 A0A064TMQ0 A0A067ALX6 A0A074TKW5 A0A080MEG8 A0A084XY41 A0A0A1A678 A0A0C7K7W3 A0A0D6I7K8 A0A0E2X7B6 A0A0F1KPK2
(80 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.
 29 A0A086JT20 A0A086JT50 A0A086JYV0 A0A086JYW5 A0A086KQG0 A0A086KQL2 A0A086LSF6 A0A086LSF6 A0A086PSR3 A0A086PST4
(19 more...)
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.
 25 A0A074TKW5 A0A086JT20 A0A086JT50 A0A086JYV0 A0A086JYW5 A0A086KQG0 A0A086KQL2 A0A086LSF6 A0A086LSF6 A0A086PSR3
(15 more...)
Long-chain-fatty-acid--[acyl-carrier-protein] ligase. [EC: 6.2.1.20]
ATP + a long-chain fatty acid + an [acyl-carrier-protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier-protein].
  • The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein.
  • Not identical with EC 6.2.1.3.
 21 A0A086JT20 A0A086JT50 A0A086JYV0 A0A086JYW5 A0A086KQG0 A0A086KQL2 A0A086LSF6 A0A086LSF6 A0A086PSR3 A0A086PST4
(11 more...)
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.
 18 A0A086JT20 A0A086JT50 A0A086JYV0 A0A086JYW5 A0A086KQG0 A0A086KQL2 A0A086LSF6 A0A086LSF6 A0A086PSR3 A0A086PST4
(8 more...)
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 14 A0A073CGA8 A0A099KCM3 A0A099KD01 B2J0Z0 B2J103 B2J683 C1F4N9 I2GT88 K9QEH2 K9XMT7
    (4 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.
    		 9 A0A073CMC6 B2IYN8 B2IYP4 B2IYP4 B2J539 F0SIS4 Q0RTS3 Q0RTS4 Q3M5Z5
    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.
    		 6 B2J016 G3J044 G4HYP5 G4HYP5 K9XLC2 K9XMT2
    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).
    		 6 A0A0S4UFU4 I4I9Q1 K9PUU3 K9XYL3 M4UND3 Q3M5M8
    Glutamate-1-semialdehyde 2,1-aminomutase. [EC: 5.4.3.8]
    (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
      		 6 B2J0F8 B2J0Y6 D8FTZ4 F9UAS6 K9VKC5 Q3M3K5
      Aspartate racemase. [EC: 5.1.1.13]
      L-aspartate = D-aspartate.
      • Also acts, at half the rate, on L-alanine.
      		 5 A0A084G055 B2IXK1 H8FPU2 K9V185 W6WGP6
      Glutamate racemase. [EC: 5.1.1.3]
      L-glutamate = D-glutamate.
        		 4 G3J046 I9NKW1 Q311J0 S0AHX7
        D-alanine--poly(phosphoribitol) ligase. [EC: 6.1.1.13]
        ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D- alanyl-poly(ribitol phosphate).
        • A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine.
        • Involved in the synthesis of teichoic acids.
        		 2 A0A095H6M2 A0A095H9B1
        Oleoyl-[acyl-carrier-protein] hydrolase. [EC: 3.1.2.14]
        Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.
        • Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.
        		 2 B7K7V0 D8G899
        Ornithine racemase. [EC: 5.1.1.12]
        L-ornithine = D-ornithine.
          		 2 G3J032 G8NU15
          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.
          		 1 Q9ZGI5
          Fatty-acid synthase. [EC: 2.3.1.85]
          Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+).
          • The animal enzyme is a multifunctional protein catalyzing the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, EC 4.2.1.59, EC 1.3.1.39 and EC 3.1.2.14.
          		 1 A0A074TKW5
          Noranthrone synthase. [EC: 2.3.1.221]
          7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinate anthrone + [acyl-carrier protein] + 7 CO(2) + 2 H(2)O.
          • A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.
          • The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase.
          		 1 Q12053
          Cyclopropane-fatty-acyl-phospholipid synthase. [EC: 2.1.1.79]
          S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl- L-homocysteine + phospholipid cyclopropane fatty acid.
          • Adds a methylene group across the 9,10 position of a Delta(9)- olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol forming a cyclopropane derivative (cf. EC 2.1.1.16).
          		 1 Q08QH1
          8-amino-7-oxononanoate synthase. [EC: 2.3.1.47]
          Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein].
          • The enzyme catalyzes the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis.
          • Pimeloyl-CoA can be used with lower efficiency.
          		 1 K9XRL8
          [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 F8AWN2
          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.
          		 1 Q9ZGI5
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