Flavoprotein pyridine nucleotide cytochrome reductase
IPR001709
Definition
Flavoprotein pyridine nucleotide cytochrome reductases PMID:1748631 (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) PMID:8027025, plant and fungal NAD(P)H:nitrate reductases [[cite:PMID:1748631], [cite:PMID:2204158]], NADH:cytochrome b5 reductases PMID:3700359, NADPH:P450 reductases PMID:1908607, NADPH:sulphite reductases PMID:2550423, nitric oxide synthases PMID:1712077, phthalate dioxygenase reductase PMID:8298460, and various other flavoproteins. Despite functional similarities, FPNCRs show no sequence similarity to NADPH:adrenodoxin reductases PMID:2924777, nor to bacterial ferredoxin:NAD+reductases and their homologues PMID:2319593. To date, 3D-structures of 4 members of the family have been solved: Spinacia oleracea (Spinach) ferredoxin:NADP+reductase PMID:1986412; Burkholderia cepacia (Pseudomonas cepacia) phthalate dioxygenase reductase PMID:8298460; the flavoprotein domain of Zea mays (Maize) nitrate reductase PMID:7812715; and Sus scrofa (Pig) NADH:cytochrome b5 reductase PMID:7890048. In all of them, the FAD-binding domain (N-terminal) has the topology of an anti-parallel β-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel β-sheet with 2 helices on each side) PMID:8298460. 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) PMID:7812715.
9 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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