Oxidoreductase FAD-binding domain

Oxidoreductase FAD-binding domain
Oxidoreductase FAD-binding domain
Identifiers
Symbol FAD_binding_6
Pfam PF00970
InterPro IPR008333
SCOP 1cne

The oxidoreductase FAD-binding domain is an evolutionary conserved protein domain.

To date, the 3D-structures of the flavoprotein domain of Zea mays nitrate reductase[1] and of pig NADH:cytochrome b5 reductase[2] have been solved. The overall fold is similar to that of ferredoxin:NADP+ reductase:[3] 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).

Examples

Human genes encoding proteins containing this domain inlclude:

References

  1. ^ Lindqvist Y, Schneider G, Campbell WH, Lu G (1994). "Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 A resolution: relationship to other flavoprotein reductases". Structure 2 (9): 809–821. PMID 7812715. 
  2. ^ Miki K, Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K (1995). "Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution". Biochemistry 34 (9): 2763–2767. doi:10.1021/bi00009a004. PMID 7893687. 
  3. ^ Karplus PA, Bruns CM (1994). "Structure-function relations for ferredoxin reductase". J. Bioenerg. Biomembr. 26 (1): 89–99. doi:10.1007/BF00763221. PMID 8027025. 

This article includes text from the public domain Pfam and InterPro IPR008333

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