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CATH Superfamily 2.30.110.10

Electron Transport, Fmn-binding Protein; Chain A

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:

"
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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 12 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
Pyridoxal 5'-phosphate synthase. [EC: 1.4.3.5]
(1) Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + NH(3) + H(2)O(2). (2) Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-phosphate + H(2)O(2).
  • In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5.
 879 A0A009ISB0 A0A009KYQ0 A0A009T259 A0A011VFC0 A0A015U3S9 A0A015UQJ1 A0A016DN73 A0A016EA88 A0A016GI20 A0A017NDY8
(869 more...)
FMN reductase (NADH). [EC: 1.5.1.42]
FMNH(2) + NAD(+) = FMN + NADH.
  • The enzyme often forms a two-component system with monooxygenases.
  • Unlike EC 1.5.1.38 and EC 1.5.1.39, 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.
 218 A0A023YVL6 A0A025CAX8 A0A026UWF8 A0A028AUV6 A0A028E0K8 A0A029I6J3 A0A029IXX4 A0A061KE72 A0A066SWF2 A0A069XLJ1
(208 more...)
Flavin reductase (NADH). [EC: 1.5.1.36]
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.
 173 A0A009S7E9 A0A023Z7M2 A0A025CZ16 A0A026V5Y1 A0A062DFS5 A0A062F3H4 A0A070F8K4 A0A070V1S8 A0A073FXT8 A0A073GZQ6
(163 more...)
FAD reductase (NADH). [EC: 1.5.1.37]
FADH(2) + NAD(+) = FAD + NADH.
  • The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD.
  • Unlike EC 1.5.1.36, the enzyme can not reduce riboflavin.
  • The enzyme does not use NADPH as acceptor.
 9 A0A072ZDW9 A0A1G5GZZ6 A0A1S1C3F4 A0A2V2TUQ5 A0A3S4N2P1 M4YFG7 O87008 Q9HWT6 W1MG08
5a,11a-dehydrotetracycline reductase. [EC: 1.3.98.4]
Tetracycline + oxidized coenzyme F420 = 5a,11a-dehydrotetracycline + reduced coenzyme F420.
  • The enzyme, characterized from the bacteria Streptomyces aureofaciens and Streptomyces rimosus, catalyzes the last step in the biosynthesis of the tetracycline antibiotics tetracycline and oxytetracycline.
 7 A0A0L8PJ91 A0A0M8RIU2 A0A0M9XFV9 A0A0X7JFP7 A0A429I1I7 A0A429JRJ9 L8EYU3
Heme oxygenase (biliverdin-IX-beta and delta-forming). [EC: 1.14.99.58]
(1) Protoheme + 3 reduced acceptor + 3 O(2) = biliverdin-IX-delta + CO + Fe(2+) + 3 acceptor + 3 H(2)O. (2) Protoheme + 3 reduced acceptor + 3 O(2) = biliverdin-IX-beta + CO + Fe(2+) + 3 acceptor + 3 H(2)O.
  • The enzyme, characterized from the bacterium Pseudomonas aeruginosa, differs from EC 1.14.15.20 in that the heme substrate is rotated by approximately 110 degrees within the active site, resulting in cleavage at a different part of the ring.
  • It forms a mixture of about 70% biliverdin-IX-delta and 30% biliverdin-IX-beta.
 7 A0A086SKF8 A0A0H3Q2T0 A0A0X1L103 A0A366AIS6 A0A366AUT9 C2HZH9 Q9KL41
4-nitrophenol 2-monooxygenase. [EC: 1.14.13.29]
4-nitrophenol + NADH + O(2) = 4-nitrocatechol + NAD(+) + H(2)O.
    		 2 D0FZR2 Q6F4M9
    4-nitrocatechol 4-monooxygenase. [EC: 1.14.13.166]
    4-nitrocatechol + NAD(P)H + O(2) = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)(+) + H(2)O.
    • The enzyme catalyzes the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite.
    • Forms a two-component system with a flavoprotein reductase.
    • The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyze EC 1.14.13.29, while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyze EC 1.14.13.167.
    		 2 D0FZR2 Q6F4M9
    NAD(P)H-hydrate epimerase. [EC: 5.1.99.6]
    (1) (6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. (2) (6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-beta-hydroxy-1,4,5,6- tetrahydronicotinamide-adenine dinucleotide phosphate.
    • The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate.
    • Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93.
    		 1 Q9LTX3
    Ferric-chelate reductase (NAD(P)H). [EC: 1.16.1.10]
    2 Fe(II)-siderophore + NAD(P)(+) + H(+) = 2 Fe(III)-siderophore + NAD(P)H.
    • The enzyme catalyzes the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron.
    • The enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus is not active with uncomplexed Fe(III).
    • Cf. EC 1.16.1.7 and EC 1.16.1.9.
    		 1 O29428
    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.
    		 1 O34138
    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 Q8KI76