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CATH Superfamily 3.40.50.12780

ANL, N-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 named:

"
N-terminal domain of ligase-like
".

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 3: Long-chain-fatty-acid--CoA ligase FadD

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).
 5927 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4 A0A023YYT4
(5917 more...)
4-coumarate--CoA ligase. [EC: 6.2.1.12]
ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA.
    		 15 A0A178W9C1 A0A178W9C1 A0A178W9C1 A0A384L454 A0A384L454 A0A384L454 B1GUZ3 B1GUZ3 Q42524 Q42524
    (5 more...)
    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.
    		 6 A0A088E3M2 A0A088E3M2 A4YDR9 A4YDR9 Q8VZF1 Q9C8D4
    Acetate--CoA ligase. [EC: 6.2.1.1]
    ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
    • Also acts on propanoate and propenoate.
    		 5 A0A088E3M2 A0A088E3M2 A4YDR9 A4YDR9 Q8VZF1
    Propionate--CoA ligase. [EC: 6.2.1.17]
    ATP + propanoate + CoA = AMP + diphosphate + propanoyl-CoA.
    • Propenoate can act instead of propanoate.
    • Not identical with EC 6.2.1.1 or EC 6.2.1.2.
    		 4 A0A088E3M2 A0A088E3M2 A4YDR9 A4YDR9
    4-hydroxybutyrate--CoA ligase (AMP-forming). [EC: 6.2.1.40]
    ATP + 4-hydroxybutanoate + CoA = AMP + diphosphate + 4-hydroxybutanoyl- CoA.
    • Isolated from the archaeon Metallosphaera sedula.
    • Involved in the 3-hydroxypropanoate/4-hydroxybutanoate cycle.
    • Cf. EC 6.2.1.56.
    		 4 A0A088E3M2 A0A088E3M2 A4YDR9 A4YDR9
    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
    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