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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-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:

"
NAD(P)-binding Rossmann-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 287896: Fatty acyl-CoA reductase 1

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
Fatty acyl-CoA reductase. [EC: 1.2.1.n2]
Hexadecanal + CoA + NADP(+) = hexadecanoyl-CoA + NADPH.
    		 2762 A0A016VBI8 A0A022PN56 A0A022PTN0 A0A022PXS1 A0A022Q0K5 A0A022R0N0 A0A022R2R6 A0A022R6J0 A0A022R760 A0A022R8E3
    (2752 more...)
    Aryl-aldehyde dehydrogenase (NADP(+)). [EC: 1.2.1.30]
    An aromatic aldehyde + NADP(+) + AMP + diphosphate + H(2)O = an aromatic acid + NADPH + ATP.
      		 2 A0A1E7VPY5 A0A1E7WVM4
      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).
      		 1 A0A0B6WU16
      Alcohol-forming fatty acyl-CoA reductase. [EC: 1.2.1.84]
      A long-chain acyl-CoA + 2 NADPH = CoA + a long-chain alcohol + 2 NADP(+).
      • The enzyme has been characterized from the plant Simmondsia chinensis (jojoba).
      • The alcohol is formed by a four-electron reduction of fatty acyl-CoA.
      • Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released.
      • The recombinant enzyme was shown to accept saturated and mono- unsaturated fatty acyl-CoAs of 16 to 22 carbons.
      		 1 Q9XGY7
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