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CATH Superfamily 3.40.50.1820

Alpha/Beta hydrolase fold, catalytic domain

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 115538: Non-ribosomal peptide synthetase modules

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
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.
 30 A0A076W660 A0A090YSX2 A0A095FE99 A0A0B5NTM9 A0A0B5R4T8 A0A0B5SIF8 A0A0D0HWD9 A0A0E1MCN7 A0A0F6FQN2 A0A0P8WI38
(20 more...)
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).
 12 A0A0D6VG20 A0A0E1LPY5 A0A0N1NI58 F5BGZ8 I2C5F1 M9U2R1 S5TK60 S5UAS3 S5UC05 S5UCA6
(2 more...)
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 9 A0A0M1QH40 A0A0N1FQP5 B2J6M7 G0Q4J3 Q0SJL7 Q3M1N0 Q3M5N4 Q3M6C6 W6W133
    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.
    		 7 A0A0M7ASL3 A0A0M9EGD5 A0A0N7M043 A0A0P1G7R6 A0A0P1GQ22 A0A0P1GXM3 A0A150KYQ2
    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.
    		 5 A0A0E1LPY5 B2J0Y5 G0Q181 I2C5F1 W6W133
    Aspartate racemase. [EC: 5.1.1.13]
    L-aspartate = D-aspartate.
    • Also acts, at half the rate, on L-alanine.
    		 5 G0Q4H1 I9NY33 K9XLR7 Q0SEB1 Q0SKF6
    Glutamate racemase. [EC: 5.1.1.3]
    L-glutamate = D-glutamate.
      		 5 A0A0N1NI58 B2IYP8 B2JBV4 K9PTF2 W4A7V5
      [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.
      		 4 D8G9C0 G0Q4J3 K9XLR7 Q3MCQ0
      N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase. [EC: 6.3.2.26]
      L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H(2)O = N-(L-5- amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate.
      • The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction.
      • Forms part of the penicillin biosynthesis pathway.
      		 2 D8G9C0 Q3MCQ0
      Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing). [EC: 1.13.12.7]
      Photinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + AMP + diphosphate + light.
      • Photinus (firefly) is a bioluminescent insect.
      • The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate.
      • The enzyme may be assayed by measurement of light emission.
      		 1 Q3M1N0
      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.
      		 1 A0A1G4LJG3
      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.
      		 1 B2JBV4
      Ribosomal-protein-alanine N-acetyltransferase. [EC: 2.3.1.128]
      Acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein N-acetyl-L-alanine.
      • A groups of enzymes in Escherichia coli that acetylate the N-terminal alanine residues of specific ribosomal proteins.
      		 1 D8GX13
      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.
      		 1 B2IYP8
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