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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 31101: 4 coumarate CoA ligase

There are 4 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
Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing). [EC: 1.13.12.7]
Photinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + AMP + diphosphate + light.
  • Photinus (firefly) is a bioluminescent insect.
  • The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate.
  • The enzyme may be assayed by measurement of light emission.
 19 A0A0B2RWE7 A0A0C6E0Y4 B7PE19 E0VSL5 H1AD96 P08659 P13129 Q01158 Q1AG35 Q1WLP6
(9 more...)
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 A0A0H4P7C4 A0A166BQX0 C0QL26 Q8EP96 Q9VCC6
4-coumarate--CoA ligase. [EC: 6.2.1.12]
ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA.
    		 3 A0A0B2RWE7 B8C078 Q54P79
    Fatty-acyl-CoA synthase. [EC: 2.3.1.86]
    Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
    • The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi- functional protein complex composed of two subunits.
    • One subunit catalyzes the reactions EC 1.1.1.100 and EC 2.3.1.41, while the other subunit catalyzes the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 4.2.1.59, EC 1.3.1.10 and EC 1.1.1.279.
    • The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
    		 1 Q9VCC6