The domain within your query sequence starts at position 188 and ends at position 499; the E-value for the Pyr_redox_2 domain shown below is 1.5e-15.

AKIALFGAGPASISCASFLARLGYSNITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIEL
MKDLGVKIICGKSLSTDEMTLSSLKENGYRAAFIGIGLPEPKKDHIFQGLTQVQGFYTSK
DFLPLVAKSSKTGMCACHSPLPSIRGAVIVLGAGDTAFDCATSALRCGALRVFIVFRKGF
VNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKDGKIVAMQFVRTEQDETGNWVEDEEQTV
RLKADVVISAFGSVLEDPKVKEALSPIKFNRWGLPEVNPETMQTSEPWVFAGGDVVGMAN
TTVESVNDGKQA

Pyr_redox_2

Pyr_redox_2
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