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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 22159: Bacitracin synthase subunit BacB

There are 7 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
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 10 O30408 O30408 O68008 O68008 O68008 O68008 R9TVM4 R9TVM4 R9TVM4 R9TVM4
    Ornithine racemase. [EC: 5.1.1.12]
    L-ornithine = D-ornithine.
      		 8 O68007 O68007 O68007 O68007 R9TZ92 R9TZ92 R9TZ92 R9TZ92
      Aspartate racemase. [EC: 5.1.1.13]
      L-aspartate = D-aspartate.
      • Also acts, at half the rate, on L-alanine.
      		 8 O68008 O68008 O68008 O68008 R9TVM4 R9TVM4 R9TVM4 R9TVM4
      Glutamate racemase. [EC: 5.1.1.3]
      L-glutamate = D-glutamate.
        		 6 I8U1X2 I8U1X2 O68006 O68006 R9TXV8 R9TXV8
        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.
        		 4 A0A080UAJ6 A0A080UAJ6 H0U5U2 H0U5U2
        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 A0A0G8EQR3 A0A0G8EQR3
        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.
        		 2 I8U1X2 I8U1X2
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