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QuickView for Flavoprotein pyridine nucleotide cytochrome reductase (biogroup)
- Description:
- Flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin:NADP+reductases (FNR), 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, 3D-structures of 4 members of the family 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). In spite of such structural similarities, the level of amino acid identity between family members is at or below the limit of significance (e.g., nitrate reductase is only 15% identical to FNR).
- Taxonomy/Path:
- InterPro : Oxidoreductase FAD/NAD(P)-binding / Flavoprotein pyridine nucleotide cytochrome reductase
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