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:

"
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 259: Sepiapterin reductase

There are 2 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
Sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming). [EC: 1.1.1.153]
(1) L-erythro-7,8-dihydrobiopterin + NADP(+) = sepiapterin + NADPH. (2) L-erythro-tetrahydrobiopterin + 2 NADP(+) = 6-pyruvoyl-5,6,7,8- tetrahydropterin + 2 NADPH.
  • This enzyme catalyzes the final step in the de novo synthesis of tetrahydrobiopterin from GTP.
  • The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin.
  • Cf. EC 1.1.1.325.
11 B0BML7 B2RYK3 B2RYK3 P18297 P18297 P35270 Q17QK8 Q54GP3 Q64105 Q7ZY31
(1 more...)
Benzil reductase ((S)-benzoin forming). [EC: 1.1.1.320]
(S)-benzoin + NADP(+) = benzil + NADPH.
  • The enzyme also reduces 1-phenylpropane-1,2-dione.
  • The enzyme from Bacillus cereus in addition reduces 1,4- naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency.
  • Formerly EC 1.1.1.n7.
1 Q8R536