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CATH Superfamily 3.40.50.80

Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module

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:

"
Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
".

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 12432: NAD(P)H-flavin reductase

There are 6 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
Aquacobalamin reductase. [EC: 1.16.1.3]
2 cob(II)alamin + NAD(+) + 2 H(2)O = 2 aquacob(III)alamin + NADH.
  • Formerly EC 1.6.99.8.
 546 A0A023L863 A0A023V4U9 A0A023Z5K5 A0A024KJI1 A0A025BWE0 A0A026RXR5 A0A026UZH8 A0A027TGB7 A0A027ZJZ0 A0A028E3F3
(536 more...)
Transferred entry: 1.5.1.38, 1.5.1.39 and 1.5.1.41. [EC: 1.5.1.29]
    		211 A0A023L863 A0A023Z5K5 A0A024KJI1 A0A025BWE0 A0A026RXR5 A0A026UZH8 A0A027TGB7 A0A027ZJZ0 A0A028E3F3 A0A029HFM5
    (201 more...)
    Riboflavin reductase (NAD(P)H). [EC: 1.5.1.41]
    Reduced riboflavin + NAD(P)(+) = riboflavin + NAD(P)H.
    • Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides.
    • Highest activity with riboflavin.
    • When NADH is used as acceptor, the enzyme can also utilize FMN and FAD as substrates, with lower activity than riboflavin.
    • When NADPH is used as acceptor, the enzyme has a very low activity with FMN and no activity with FAD.
    • Formerly EC 1.5.1.29 and EC 1.6.8.1.
    		 203 A0A023Z5K5 A0A024KJI1 A0A025BWE0 A0A026RXR5 A0A026UZH8 A0A027TGB7 A0A027ZJZ0 A0A028E3F3 A0A029HFM5 A0A029IH94
    (193 more...)
    FMN reductase (NADPH). [EC: 1.5.1.38]
    FMNH(2) + NADP(+) = FMN + NADPH.
    • The enzymes from bioluminescent bacteria contain FMN, while the enzyme from Escherichia coli does not.
    • The enzyme often forms a two-component system with monooxygenases such as luciferase.
    • Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor.
    • While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity.
    • Formerly EC 1.5.1.29 and EC 1.6.8.1.
    		 2 A0A0U5LSX6 J6IIR1
    FMN reductase (NAD(P)H). [EC: 1.5.1.39]
    FMNH(2) + NAD(P)(+) = FMN + NAD(P)H.
    • The enzyme can utilize NADH and NADPH with similar reaction rates.
    • Different from EC 1.5.1.42 and EC 1.5.1.38.
    • The luminescent bacterium Vibrio harveyi possesses all three enzymes, while the bacterium Aliivibrio fischeri contains only this non- specific type.
    • Also reduces riboflavin and FAD, but more slowly.
    • Formerly EC 1.5.1.29 and EC 1.6.8.1.
    		 1 V5Z3P6
    Flavin reductase (NADPH). [EC: 1.5.1.30]
    Reduced riboflavin + NADP(+) = riboflavin + NADPH.
    • The enzyme from Entamoeba histolytica reduces riboflavin and galactoflavin, and, more slowly, FMN and FAD.
    • NADH is oxidized more slowly than NADPH.
    • Formerly EC 1.6.8.2.
    		 1 A0A085U6N3