The domain within your query sequence starts at position 4 and ends at position 262; the E-value for the Pyr_redox_2 domain shown below is 2.9e-12.



PFAM accession number:PF07992
Interpro abstract (IPR023753):

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 [ (PUBMED:2319593) (PUBMED:1404382) (PUBMED:2067578) ]. 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 [ (PUBMED:2067578) ].

Despite functional similarities, oxidoreductases of this family show no sequence similarity with adrenodoxin reductases [ (PUBMED:2924777) ] and flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) [ (PUBMED:1748631) ]. Assuming that disulphide reductase activity emerged later, during divergent evolution, the family can be referred to as FAD-dependent pyridine nucleotide reductases, FADPNR.

To date, 3D structures of glutathione reductase [ (PUBMED:3656429) ], thioredoxin reductase [ (PUBMED:2067578) ], mercuric reductase [ (PUBMED:2067577) ], lipoamide dehydrogenase [ (PUBMED:1880807) ], trypanothione reductase [ (PUBMED:1924336) ] and NADH peroxidase [ (PUBMED:1942054) ] have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta 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 [ (PUBMED:7411611) ].

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.

GO process:oxidation-reduction process (GO:0055114)
GO function:oxidoreductase activity (GO:0016491)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Pyr_redox_2