Description

IPR023753 is a FAD/NAD(P)-binding domain.

<p>This entry describes the FAD binding domain which has a nested NADH binding domain and is found in both class I and class II oxidoreductases.</p> <p>FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase, trypanothione reductase, lipoamide dehydrogenase, mercuric reductase, thioredoxin reductase, alkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases, in particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase, putidaredoxin reductase, terpredoxin reductase, ferredoxin-NAD+ reductase components of benzene 1,2-dioxygenase, toluene 1,2-dioxygenase, chlorobenzene dioxygenase, biphenyl dioxygenase), NADH oxidase and NADH peroxidase [[cite:PUB00003255], [cite:PUB00003296], [cite:PUB00004100]]. Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites, suggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently [[cite:PUB00004100]].</p> <p>Despite functional similarities, oxidoreductases of this family show no sequence similarity with adrenodoxin reductases [[cite:PUB00001372]] and flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) [[cite:PUB00002674]]. Assuming that disulphide reductase activity emerged later, during divergent evolution, the family can be referred to as FAD-dependent pyridine nucleotide reductases, FADPNR.</p> <p>To date, 3D structures of glutathione reductase [[cite:PUB00003219]], thioredoxin reductase [[cite:PUB00004100]], mercuric reductase [[cite:PUB00004099]], lipoamide dehydrogenase [[cite:PUB00003272]], trypanothione reductase [[cite:PUB00004756]] and NADH peroxidase [[cite:PUB00003273]] have been solved. The enzymes share similar tertiary structures based on a doubly-wound α/β fold, but the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly. By contrast with the FPNCR family, the folds of the FAD- and NAD(P)H-binding domains are similar, suggesting that the domains evolved by gene duplication [[cite:PUB00003195]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 223