NAD(P)H oxidase superfamily

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Last update: 2021-12-02 (Bruno Savelli)

Ferric Reductase (FRE)
Ferric reduction oxidase/NADPH oxidase-like (FRO)
NADPH oxidase (NOx/RBOH)

Description

NAD(P)H oxidases belong to a superfamily of flavocytochromes enzymes that catalyze the production of superoxide (O2) by the one electron reduction of oxygen using NAD(P)H as the electron donor
2O2+NAD(P)H → 2.O2 + NAD(P)+ + H+


Ferric Reductase (FRE)



Ferric reduction oxidase/NADPH oxidase-like (FRO): FRO were identified based on their sequences similarity to the yeast ferric reductases (FRE), as well as to a subunit of the human NADPH oxidase (NOx, gp91phox). They allow the reduction of ferric iron to ferrous iron at the root surface.


NADPH oxidase (NOx/RBOH): In Human the complex include NOx (isoforms 1 to 5) and DuOx (Dual oxidase which contains Peroxidase and NOx domains).


Profiles

Ferric Reductase : Pfam: PF07992
Pyridine nucleotide-disulphide oxidoreductase (Common with GR family) Interpro: IPR023753
FAD/NAD(P)-binding domain
NADH oxidase : Pfam: PF07992
Pyridine nucleotide-disulphide oxidoreductase (Common with GR family) Interpro: IPR023753
FAD/NAD(P)-binding domain
NADPH oxidase (NOx/RBOH): Pfam: PF08022
FAD_binding_8; PF01794
Ferric_reduct;PF08030
NAD_binding_6 and PF08414
NADPH_Ox. (Specific NOx Interpro: IPR000778
Cyt_b245_heavy_chain; IPR011992 EF-hand-dom_pair; IPR000778 EF_Hand_1_Ca_BS; IPR002048 EF_hand_dom; IPR013112 FAD-bd_8; IPR017927 Fd_Rdtase_FAD-bd; IPR013130 Fe3_Rdtase_TM_dom; IPR013121 Fe_red_NAD-bd_6; IPR013623 NADPH_Ox and IPR017938 Riboflavin_synthase-like_b-brl.
Ferric reduction oxidase/NADPH oxidase-like (FRO) : Pfam: PF08022
FAD_binding_8; PF01794
Ferric_reduct;PF08030
NAD_binding_6 Interpro: IPR000778 EF_Hand_1_Ca_BS; IPR013112 FAD-bd_8; IPR017927 Fd_Rdtase_FAD-bd; IPR013130 Fe3_Rdtase_TM_dom; IPR013121 Fe_red_NAD-bd_6; IPR017938 Riboflavin_synthase-like_b-brl.

Literature

Jain A, Wilson GT, Connolly EL. The diverse roles of FRO family metalloreductases in iron and copper homeostasis. Front Plant Sci. 2014 Mar 21;5:100. PMID: 24711810