SMART: Pfam domain FAD_binding

The domain within your query sequence starts at position 80 and ends at position 177; the E-value for the FAD_binding_6 domain shown below is 8.2e-25.

AFHISTMEKVTKDTYLVRFTLPGNSRLGLRPGQHLILRGVVDGLEIQRAYTPISPVTAEG
YFDVLIKCYRTGLMSQYVESWRTGDTAFWRGPFGSFLY

FAD_binding_6

PFAM accession number:	PF00970
Interpro abstract (IPR008333):	These sequences represent the FAD-binding domain found in NADH:cytochrome b5 reductases and nitrate reductases. To date, the 3D-structures of the flavoprotein domain of Zea mays (Maize) nitrate reductase [ (PUBMED:7812715) ] and of pig NADH:cytochrome b5 reductase [ (PUBMED:7893687) ] have been solved. The overall fold is similar to that of ferredoxin:NADP ⁺ reductase [ (PUBMED:8027025) ]: the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).

PFAM accession number:

PF00970

Interpro abstract (IPR008333):

These sequences represent the FAD-binding domain found in NADH:cytochrome b5 reductases and nitrate reductases.

To date, the 3D-structures of the flavoprotein domain of Zea mays (Maize) nitrate reductase [ (PUBMED:7812715) ] and of pig NADH:cytochrome b5 reductase [ (PUBMED:7893687) ] have been solved. The overall fold is similar to that of ferredoxin:NADP ⁺ reductase [ (PUBMED:8027025) ]: the FAD-binding domain (N-terminal) has the topology of an anti-parallel beta-barrel, while the NAD(P)-binding domain (C-terminal) has the topology of a classical pyridine dinucleotide-binding fold (i.e. a central parallel beta-sheet flanked by 2 helices on each side).

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FAD_binding_6