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:

Electron Transport, Fmn-binding Protein; Chain A

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 14387: 4-hydroxyphenylacetate 3-monooxygenase reductase c...

There are 8 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
FMN reductase (NADH). [EC:]
FMNH(2) + NAD(+) = FMN + NADH.
  • The enzyme often forms a two-component system with monooxygenases.
  • Unlike EC and EC, this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed.
  • While FMN is the preferred substrate, FAD can also be used with much lower activity.
715 A0A014M6I9 A0A016XDU1 A0A023WPB6 A0A023YVL6 A0A024IXY4 A0A024KUN3 A0A025CAX8 A0A026RUS4 A0A026UWF8 A0A027U5C8
(705 more...)
Flavin reductase (NADH). [EC:]
Reduced flavin + NAD(+) = flavin + NADH.
  • The enzyme from Escherichia coli W catalyzes the reduction of free flavins by NADH.
  • The enzyme has similar affinity to FAD, FMN and riboflavin.
  • Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH.
284 A0A023Z7M2 A0A025CZ16 A0A026V5Y1 A0A027U2T8 A0A028APZ1 A0A028DN51 A0A029P0Y1 A0A060VCM0 A0A064SWT0 A0A068H5K8
(274 more...)
4-hydroxyphenylacetate 3-monooxygenase. [EC:]
4-hydroxyphenylacetate + FADH(2) + O(2) = 3,4-dihydroxyphenylacetate + FAD + H(2)O.
  • The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds.
  • The enzyme uses FADH(2) as a substrate rather than a cofactor.
  • FADH(2) is provided by EC
  • Formerly EC
248 A0A022PHG8 A0A023Z7M2 A0A025CZ16 A0A026V5Y1 A0A027U2T8 A0A029P0Y1 A0A064SWT0 A0A068H5K8 A0A070D7W9 A0A070F8K4
(238 more...)
Penicillin amidase. [EC:]
Penicillin + H(2)O = a carboxylate + 6-aminopenicillanate.
    96 A0A023Z7M2 A0A025CZ16 A0A026V5Y1 A0A027U2T8 A0A029P0Y1 A0A064SWT0 A0A070D7W9 A0A070F8K4 A0A070V1S8 A0A073FXT8
    (86 more...)
    Flavin reductase (NADPH). [EC:]
    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
    25 A0A084ZMU9 A0A085GP40 A0A085H7A7 A0A085HP69 A0A085HSC8 A0A085IB56 A0A097R5C2 A0A0B8ZZ12 A0A0C5WCK4 A0A0K0HVF5
    (15 more...)
    Riboflavin reductase (NAD(P)H). [EC:]
    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 and EC
    25 A0A084ZMU9 A0A085GP40 A0A085H7A7 A0A085HP69 A0A085HSC8 A0A085IB56 A0A097R5C2 A0A0B8ZZ12 A0A0C5WCK4 A0A0K0HVF5
    (15 more...)
    Transferred entry: [EC:]
      7 A0A0H2YK50 A0A0H3B3U4 A0A0M1V5R6 A0A0U1ESA4 A0A0U1QXV1 Q66BX0 Q7CHW0
      FAD reductase (NADH). [EC:]
      FADH(2) + NAD(+) = FAD + NADH.
      • The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD.
      • Unlike EC, the enzyme can not reduce riboflavin.
      • The enzyme does not use NADPH as acceptor.
      5 A0A072ZDW9 A0A0P1D751 A0A1G5GZZ6 Q9HWT6 W1MG08