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CATH Superfamily 1.10.1200.10

ACP-like

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:

"
ACP-like
".

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 24074: Polyketide synthase, putative (JCVI)

There are 16 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.
 36 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A100JMV6 A0A100JMV6 A0A171A6J3 A0A171A6J3 B3MLJ5 B3MLJ5
(26 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.
 36 A0A0C5V8V4 A0A0C5V8V4 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A171A6J3 A0A171A6J3 B3MLJ5 B3MLJ5
(26 more...)
[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.
 36 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A171A6J3 A0A171A6J3 B3MLJ5 B3MLJ5 B4KI46 B4KI46
(26 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.
 34 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A171A6J3 A0A171A6J3 B2J541 B2J541 B3MLJ5 B3MLJ5
(24 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.
 32 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A171A6J3 A0A171A6J3 B3MLJ5 B3MLJ5 B4KI46 B4KI46
(22 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.
 30 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A171A6J3 A0A171A6J3 B3MLJ5 B3MLJ5 B4KI46 B4KI46
(20 more...)
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.
 26 A0A0J9QVK6 A0A0J9QVK6 A0A0J9TEH0 A0A0J9TEH0 A0A171A6J3 A0A171A6J3 B3MLJ5 B3MLJ5 B4KI46 B4KI46
(16 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.
 24 A0A063BLL2 A0A063BLL2 A0A0C5QFG3 A0A0C5QFG3 A0A0C5QFG3 A0A0C5QFG3 B2J541 B2J541 B8LUA8 B8LUA8
(14 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.
 22 A0A171A6J3 A0A171A6J3 A0A1L1YNR3 A0A1L1YNR3 B7Z001 B7Z001 E0W0Z3 E0W0Z3 M9PB21 M9PB21
(12 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.
 10 A0A063BLL2 A0A063BLL2 E0W0Z3 E0W0Z3 K9XMT2 K9XMT2 Q39J94 Q39J94 W6WTW1 W6WTW1
Enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific). [EC: 1.3.1.39]
An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADPH.
  • This enzyme completes each cycle of fatty acid elongation by catalyzing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl- carrier protein.
  • It is one of the activities of EC 2.3.1.85.
  • The mammalian enzyme is Re-specific with respect to NADP(+) (cf. EC 1.3.1.10 and and EC 1.3.1.104).
 6 P12785 P12785 P19096 P19096 P49327 P49327
Glutamate racemase. [EC: 5.1.1.3]
L-glutamate = D-glutamate.
    		 4 A0A0C5QFG3 A0A0C5QFG3 A0A0C5QFG3 A0A0C5QFG3
    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).
    		 2 A0A150KYP0 A0A150KYP0
    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.
    		 2 A0A0J6WDF3 A0A0J6WDF3
    Transferred entry: 4.2.1.59. [EC: 4.2.1.61]
      		2 E0W0Z3 E0W0Z3
      Acetyl-CoA C-acetyltransferase. [EC: 2.3.1.9]
      2 acetyl-CoA = CoA + acetoacetyl-CoA.
        		 2 A0A0S2CHA9 A0A0S2CHA9
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