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CATH Superfamily 3.30.300.30

ANL, C-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_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 8: 2,3-dihydroxybenzoate-AMP ligase

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
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).
 110 A0A045I108 A0A045I108 A0A045I108 A0A045I108 A0A045I108 A0A045I108 A0A045I108 A0A045I108 A0A045I108 A0A045I108
(100 more...)
Firefly luciferase. [EC: 1.13.12.7]
D-firefly luciferin + O(2) + ATP = firefly oxyluciferin + CO(2) + AMP + diphosphate + light.
  • The enzyme, which is found in fireflies (Lampyridae), is responsible for their biolouminescence.
  • The reaction begins with the formation of an acid anhydride between the carboxylic group of D-firefly luciferin and AMP, with the release of diphosphate.
  • An oxygenation follows, with release of the AMP group and formation of a very short-lived peroxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO(2) molecule.
  • The spontaneous breakdown of the dioxetanone (rather than the hydrolysis of the adenylate) releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of oxyluciferin.
  • The excited luciferin then emits a photon, returning to its ground state.
  • The enzyme has a secondary acyl-CoA ligase activity when acting on L-firefly luciferin.
 5 H1AD96 H1AD96 P08659 P08659 Q26304
Medium-chain acyl-CoA ligase. [EC: 6.2.1.2]
ATP + a medium-chain fatty acid + CoA = AMP + diphosphate + a medium- chain acyl-CoA.
  • Acts on fatty acids from C(4) to C(11) and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids.
  • The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives.
 2 Q8VZF1 Q9C8D4
O-succinylbenzoate--CoA ligase. [EC: 6.2.1.26]
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA.
    		 2 P58730 Q71YZ5
    Benzoate--CoA ligase. [EC: 6.2.1.25]
    ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA.
    • Also acts on 2-, 3- and 4-fluorobenzoate, but only very slowly on the corresponding chlorobenzoates.
    		 1 Q9SS01
    3-(methylthio)propionyl--CoA ligase. [EC: 6.2.1.44]
    ATP + 3-(methylthio)propanoate + CoA = AMP + diphosphate + 3-(methylthio)propanoyl-CoA.
    • The enzyme is part of a dimethylsulfoniopropanoate demethylation pathway in the marine bacteria Ruegeria pomeroyi and Pelagibacter ubique.
    • It also occurs in some nonmarine bacteria capable of metabolizing dimethylsulfoniopropionate (e.g. Burkholderia thailandensis, Pseudomonas aeruginosa, and Silicibacter lacuscaerulensis).
    		 1 Q5LRT0
    2-hydroxy-7-methoxy-5-methyl-1-naphthoate--CoA ligase. [EC: 6.2.1.43]
    ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA = AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA.
    • The enzyme from the bacterium Streptomyces carzinostaticus is involved in the attachment of the 2-hydroxy-7-methoxy-5-methyl-1- naphthoate moiety of the antibiotic neocarzinostatin.
    • In vitro the enzyme also catalyzes the activation of other 1-naphthoic acid analogs, e.g. 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate.
    		 1 Q84HC5
    Acetate--CoA ligase. [EC: 6.2.1.1]
    ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
    • Also acts on propanoate and propenoate.
    		 1 Q8VZF1