Ferredoxin--NADP reductase, bacteria (IPR033892)

Short name: FNR_bac

Overlapping homologous superfamilies

Family relationships



Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH [PMID: 15134648, PMID: 12709048].

This family consists of Ferredoxin--NADP reductase from bacteria [PMID: 8449868, PMID: 16128574].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004324 ferredoxin-NADP+ reductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.