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CATH Superfamily 3.50.50.60

FAD/NAD(P)-binding 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:

"
FAD/NAD(P)-binding 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 824: 1-hydroxycarotenoid 3,4-desaturase

There are 1 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
1-hydroxycarotenoid 3,4-desaturase. [EC: 1.3.99.27]
1-hydroxy-1,2-dihydrolycopene + acceptor = 1-hydroxy-3,4-didehydro-1,2- dihydrolycopene + reduced acceptor.
  • The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides prefer the acyclic carotenoids (e.g. 1-hydroxy-1,2- dihydroneurosporene, 1-hydroxy-1,2-dihydrolycopene) as substrates.
  • The conversion rate for the 3,4-desaturation of the monocyclic 1'-hydroxy-1',2'-dihydro-gamma-carotene is lower.
  • The enzyme from the marine bacterium strain P99-3 shows high activity with the monocyclic carotenoid 1'-hydroxy-1',2'-dihydro-gamma- carotene.
  • The enzyme from Rhodobacter sphaeroides utilizes molecular oxygen as the electron acceptor in vitro.
  • However, oxygen is unlikely to be the natural electron acceptor under anaerobic conditions.
 1 Q7WT72
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