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CATH Superfamily 3.30.559.10

Chloramphenicol acetyltransferase-like 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 named:

"
Chloramphenicol acetyltransferase-like domain
".

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 22362: Siderophore non-ribosomal peptide synthetase

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.
 200 A0A066ZX53 A0A066ZX53 A0A067AEU8 A0A067AEU8 A0A076W0E5 A0A076W0E5 A0A076W0E5 A0A076W0E5 A0A080UAJ6 A0A080UAJ6
(190 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).
 144 A0A076LVL7 A0A076LVL7 A0A0A1I1G1 A0A0A1I1G1 A0A0C5VLD3 A0A0C5VLD3 A0A0C5VMD5 A0A0C5VMD5 A0A0C5VUT5 A0A0C5VUT5
(134 more...)
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 138 A0A068QRD8 A0A068QRD8 A0A068QUR4 A0A068QUR4 A0A068R1Z4 A0A068R1Z4 A0A068R289 A0A068R289 A0A068R289 A0A068R289
    (128 more...)
    Aspartate racemase. [EC: 5.1.1.13]
    L-aspartate = D-aspartate.
    • Also acts, at half the rate, on L-alanine.
    		 116 A0A031HMY9 A0A031HMY9 A0A098BKA4 A0A098BKA4 A0A0A8USD9 A0A0A8USD9 A0A0A8USD9 A0A0A8USD9 A0A0D5M7Y4 A0A0D5M7Y4
    (106 more...)
    Ornithine racemase. [EC: 5.1.1.12]
    L-ornithine = D-ornithine.
      		 70 A0A068QRD8 A0A068QRD8 A0A068QUR4 A0A068QUR4 A0A068R1Z4 A0A068R1Z4 A0A068R289 A0A068R289 A0A068R289 A0A068R289
      (60 more...)
      Glutamate racemase. [EC: 5.1.1.3]
      L-glutamate = D-glutamate.
        		 48 A0A1C4DPF8 A0A1C4DPF8 A0A1C4FFB3 A0A1C4FFB3 A0A1D3P057 A0A1D3P057 A0A1E7ZRY0 A0A1E7ZRY0 A0A1E8A4Z7 A0A1E8A4Z7
        (38 more...)
        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.
        		 42 A0A073CET2 A0A073CET2 B2IXJ7 B2IXJ7 B2IXJ7 B2IXJ7 E2Q5R1 E2Q5R1 H0RWK9 H0RWK9
        (32 more...)
        L-aminoadipate-semialdehyde dehydrogenase. [EC: 1.2.1.31]
        (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H.
          		 16 A0A077N6G7 A0A077N6G7 A5EAZ3 A5EAZ3 A5EHY6 A5EHY6 B2J684 B2J684 D3UWT1 D3UWT1
          (6 more...)
          D-arabinose isomerase. [EC: 5.3.1.3]
          D-arabinose = D-ribulose.
          • The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene- diol mechanism.
          • The enzyme catalyzes the aldose-ketose isomerization of several sugars.
          • Most enzymes also catalyze the reaction of EC 5.3.1.25.
          • The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose.
          • Cf. EC 5.3.1.4.
          		 12 E0RJP4 E0RJP4 E0RJP4 E0RJP4 E0RJP4 E0RJP4 E0RJP4 E0RJP4 E0RJP4 E0RJP4
          (2 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.
          		 10 I2C681 I2C681 I2C683 I2C683 I2C685 I2C685 I2CAP2 I2CAP2 Q3MCQ0 Q3MCQ0
          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.
          		 6 B2IXK1 B2IXK1 G3J042 G3J042 K9QEH2 K9QEH2
          4-hydroxybenzoate--CoA ligase. [EC: 6.2.1.27]
          ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA.
            		 4 W6VXV4 W6VXV4 W6VXV4 W6VXV4
            Acetate--CoA ligase. [EC: 6.2.1.1]
            ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
            • Also acts on propanoate and propenoate.
            		 2 W3ZZ15 W3ZZ15
            Transferred entry: 2.1.1.319, 2.1.1.320, 2.1.1.321 and 2.1.1.322. [EC: 2.1.1.125]
              		2 G2E5D1 G2E5D1
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