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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 52671: Fatty acid synthase Fas

There are 14 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.
 131 A0A059MRB8 A0A080N4A6 A0A086YYH8 A0A086ZER7 A0A086ZIZ0 A0A086ZLP7 A0A087A8U1 A0A087AG86 A0A087ANV1 A0A087AXX9
(121 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.
 41 A0A059MRB8 A0A080N4A6 A0A086YYH8 A0A086ZER7 A0A086ZIZ0 A0A086ZLP7 A0A087A8U1 A0A087AG86 A0A087ANV1 A0A087AXX9
(31 more...)
Fatty-acyl-CoA synthase. [EC: 2.3.1.86]
Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
  • The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi- functional protein complex composed of two subunits.
  • One subunit catalyzes the reactions EC 1.1.1.100 and EC 2.3.1.41, while the other subunit catalyzes the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 4.2.1.59, EC 1.3.1.10 and EC 1.1.1.279.
  • The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
 38 A0A080N4A6 A0A086YYH8 A0A086ZER7 A0A086ZIZ0 A0A086ZLP7 A0A087A8U1 A0A087AG86 A0A087ANV1 A0A087AXX9 A0A087BF99
(28 more...)
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.
 16 A0A0B6TI31 A0A0D6GTV3 A0A0F5D8K4 A0A0P4UN86 A2QSJ3 A2QYP5 C1A1U6 C1AVV2 C3PIL8 D3R3L8
(6 more...)
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.
 11 A0A0T9FSH2 A0A143Q5N7 A0A143QRU2 A0A165MH67 A0A173WZQ3 A0A173XBC7 A0A174AB17 A0A174BA80 A0A1F2PUQ8 A0A1N5I1K7
(1 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.
 10 A0A059MRB8 A0A0E9DZ50 A0A0N9YE58 A0A173WZQ3 A0A173XBC7 A0A174AB17 C3PIL8 D3R3L8 N1M581 V6XYC9
[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.
 7 A0A059MRB8 A0A0A1FSM8 A0A0N9YE58 C3PIL8 K0VSI7 N1M581 V6XYC9
3-hydroxyacyl-[acyl-carrier-protein] dehydratase. [EC: 4.2.1.59]
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O.
  • This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria.
  • The enzyme uses fatty acyl thioesters of ACP in vivo.
  • Different forms of the enzyme may have preferences for substrates with different chain length.
  • For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length.
  • Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14.
  • Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0).
  • FabZ, but not FabA, can also accept unsaturated substrates.
  • Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61.
 6 A0A059MRB8 A0A0N9YE58 C3PIL8 D3R3L8 N1M581 V6XYC9
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.
 4 A0A059MRB8 A0A0N9YE58 N1M581 V6XYC9
Exopolyphosphatase. [EC: 3.6.1.11]
(Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate.
    		 2 E8JLE9 L8F7U6
    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 C3PIL8 D3R3L8
    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 C3PIL8 D3R3L8
    Holo-[acyl-carrier-protein] synthase. [EC: 2.7.8.7]
    CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].
    • All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active.
    • The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain.
    • The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier- proteins from prokaryotes.
    • Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.
    		 1 A0A0P4U2V1
    Glutamate N-acetyltransferase. [EC: 2.3.1.35]
    N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- glutamate.
    • Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
    		 1 D3R3L8
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