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CATH Superfamily 3.20.20.70

Aldolase class I

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:

"
Aldolase class I
".

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 119653: Fatty acid synthase beta subunit

There are 10 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
[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.
 30 A0A084G1R6 A0A084G1R6 A0A0F4Z5H9 A0A0F4Z5H9 A0A1D8N7V8 A0A1D8N7V8 A2QYP6 A2QYP6 B8LZM2 B8LZM2
(20 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.
 28 A0A084G1R6 A0A084G1R6 A0A1D8N7V8 A0A1D8N7V8 A2QTD8 A2QTD8 A2QYP6 A2QYP6 B9WGW5 B9WGW5
(18 more...)
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.
 26 A0A084G1R6 A0A084G1R6 A0A0L1HUE5 A0A0L1HUE5 A0A0P4U8E6 A0A0P4U8E6 A0A1D8N7V8 A0A1D8N7V8 A2QYP6 A2QYP6
(16 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.
 24 A0A0H3LD53 A0A0H3LD53 A0A0T9Z6H1 A0A0T9Z6H1 A0A1K3ET64 A0A1K3ET64 A0A1K4K6X5 A0A1K4K6X5 A0A1K7EE29 A0A1K7EE29
(14 more...)
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.
 22 A0A084G1R6 A0A084G1R6 A0A0F8B4X8 A0A0F8B4X8 A0A1D8N7V8 A0A1D8N7V8 B9WGW5 B9WGW5 N1P0M8 N1P0M8
(12 more...)
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.
 22 A0A084G1R6 A0A084G1R6 A0A0L1HUE5 A0A0L1HUE5 A0A0P4U8E6 A0A0P4U8E6 A0A1D8N7V8 A0A1D8N7V8 N1P0M8 N1P0M8
(12 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.
 20 A0A1D8N7V8 A0A1D8N7V8 A2QYP6 A2QYP6 B9WGW5 B9WGW5 N1P0M8 N1P0M8 P07149 P07149
(10 more...)
Transferred entry: 4.2.1.59. [EC: 4.2.1.61]
    		4 A2QYP6 A2QYP6 B9WGW5 B9WGW5
    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.
    		 4 A0A0L1HUE5 A0A0L1HUE5 A0A0P4U8E6 A0A0P4U8E6
    Nitronate monooxygenase. [EC: 1.13.12.16]
    Ethylnitronate + O(2) = acetaldehyde + nitrite + other products.
    • Previously classified as EC 1.13.11.32, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms.
    • The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor.
    • Neither hydrogen peroxide nor superoxide were detected during enzyme turnover.
    • Active toward linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, toward propyl-2-nitronate.
    • The enzyme from N.crassa can also utilize neutral nitroalkanes, but with lower activity.
    • Formerly EC 1.13.11.32.
    		 2 A0A0L1HUE5 A0A0L1HUE5
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