NAD(P)H oxidase superfamily

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Last update: 2019-05-29 (Christophe Dunand)

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

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.

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).

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