LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | Ferredoxin reductase is a member of the flavoprotein pyridine nucleotide cytochrome reductases [ ] (FPNCRs) that 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 [ ] various other flavoproteinsDespite 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 [ ] Zea mays (Maize) nitrate reductase flavoprotein domain [ ] Sus scrofa (Pig) NADH:cytochrome b5 reductase [ ]. 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) [].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 |
