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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 22492: Nonribosomal peptide synthase GliP2

There are 5 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
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 A0A150KZ21
Glutamate racemase. [EC: 5.1.1.3]
L-glutamate = D-glutamate.
    		 2 A0A0C5QFG3 I9NKI8
    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.
    		 1 A0A0C5QFG3
    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.
    		 1 P27743
    [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.
    		 1 A0A1G4LJD9
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