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: waiting to be named.

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 16331: NADPH-dependent FMN reductase

There are 7 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
NAD(P)H dehydrogenase (quinone). [EC: 1.6.5.2]
NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone.
  • The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone.
  • The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.
  • Formerly EC 1.6.99.2.
324 A0A023Z571 A0A023Z571 A0A025BZJ4 A0A025BZJ4 A0A026V0Z3 A0A026V0Z3 A0A028AFY9 A0A028AFY9 A0A028DR15 A0A028DR15
(314 more...)
Azobenzene reductase. [EC: 1.7.1.6]
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP(+) = 4-(dimethylamino)azobenzene + 2 NADPH.
  • The reaction occurs in the reverse direction to that shown above.
  • Other azo dyes, such as Methyl Red, Rocceline, Solar Orange and Sumifix Black B can also be reduced.
  • Formerly EC 1.6.6.7.
276 A0A023Z571 A0A023Z571 A0A025BZJ4 A0A025BZJ4 A0A037YN28 A0A037YN28 A0A069Q4G0 A0A069Q4G0 A0A070URH5 A0A070URH5
(266 more...)
[Acyl-carrier-protein] phosphodiesterase. [EC: 3.1.4.14]
Holo-[acyl-carrier-protein] + H(2)O = 4'-phosphopantetheine + apo-[acyl- carrier-protein].
  • The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier-protein (ACP) and short- chain ACPs over the medium- and long-chain species.
  • Deletion of the gene encoding this enzyme abolishes ACP prosthetic- group turnover in vivo.
  • Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7.
40 A0A070FCE4 A0A070FCE4 B3WVF1 B3WVF1 D7XJH0 D7XJH0 D7YM04 D7YM04 E1HVN1 E1HVN1
(30 more...)
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.
30 A0A080T0K7 A0A080T0K7 A0A0E1CLW2 A0A0E1CLW2 A0A0H3GV94 A0A0H3GV94 A0A0J2GNR2 A0A0J2GNR2 A0A0M1THI2 A0A0M1THI2
(20 more...)
Fumarate reductase (quinol). [EC: 1.3.5.4]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme, which is found in anaerobic and facultative organisms such as bacteria, parasitic helminthes, and lower marine organisms, utilizes low potential quinols, such as menaquinol and rhodoquinol, to reduce fumarate as the final step of an anaerobic respiratory chain.
  • The enzyme is known as complex II of the electron transfer chain, similarly to EC 1.3.5.1, to which it is closely related.
4 A0A1A0CJT3 A0A1A0CJT3 H1US56 H1US56
Transferred entry: 1.5.1.38, 1.5.1.39 and 1.5.1.41. [EC: 1.5.1.29]
    2 A4U0J1 A4U0J1
    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.
    2 Q9USJ6 Q9USJ6