| Type: | Family | Name: | Ferredoxin--NADP reductase |
| Description: | Ferredoxin reductase is a member of the flavoprotein pyridine nucleotide cytochrome reductases [] (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. Ferredoxin reductase catalyzes the final step of electron transfer to make NADPH and ATP in plant chloroplasts during photosynthesis. Other family members include plant and fungal NAD(P)H:nitrate reductases [, ], NADH:cytochrome b5 reductases [], NADPH:P450 reductases [], NADPH:sulphite reductases [], nitric oxide synthases [], phthalate dioxygenase reductase [], and various other flavoproteins.Despite functional similarities, FPNCRs show no sequence similarity to NADPH:adrenodoxin reductases [], nor to bacterial ferredoxin:NAD reductases and their homologues []. To date, structures for a number of family members have been solved: Spinacia oleracea(Spinach) ferredoxin:NADP reductase []; Burkholderia cepacia(Pseudomonas cepacia) phthalate dioxygenase reductase []; the flavoprotein domain of Zea mays(Maize) nitrate reductase []; and Sus scrofa(Pig) NADH:cytochrome b5 reductase []. In all of them, the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet with 2 helices on each side) [].Proteins in this family also include benzoyl-CoA oxygenase component A (BoxA), which forms a complex with BoxB that catalyses the aerobic reduction/oxygenation of the aromatic ring of benzoyl-CoA to form 2,3-dihydro-2,3-dihydroxybenzoyl-CoA. BoxA also acts as a reductase that uses NADPH to reduce the oxygenase component BoxB. BoxAB does not act on NADH or benzoate []. | Short Name: | FNR |
