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CATH Superfamily 2.30.38.10

Luciferase; Domain 3

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:

"
Luciferase; Domain 3
".

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 31091: Non-ribosomal peptide synthetase modules

There are 8 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.
    		 17 A0A099K8T5 A0A0K1EK18 A0A0M0H4M2 A0A1A5VH98 A0A1G4LJR5 B4AIX0 C0ZDA5 C0ZDA6 E0RLJ1 E1UL90
    (7 more...)
    Aspartate racemase. [EC: 5.1.1.13]
    L-aspartate = D-aspartate.
    • Also acts, at half the rate, on L-alanine.
    		 6 A0A099K8T5 A0A0M0L305 A0A1G4LJR5 B4AIX0 G4NWW4 I9NU71
    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).
    		 5 A0A0D6V451 A0A0D6V6H2 A0A150KSG7 A0A150KTM0 A0A150KVZ8
    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.
    		 3 A0A080UAJ6 A0A090YA11 A0A095RGG2
    Glutamate racemase. [EC: 5.1.1.3]
    L-glutamate = D-glutamate.
      		 3 G7MBA8 I8U1X2 I8U1X2
      Ornithine racemase. [EC: 5.1.1.12]
      L-ornithine = D-ornithine.
        		 2 E1UL88 W1J3Z6
        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
        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 T2IYX3 T2JZR3