Oxidoreductase FAD-binding domain
| Oxidoreductase FAD-binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | FAD_binding_6 | ||||||||
| Pfam | PF00970 | ||||||||
| InterPro | IPR008333 | ||||||||
| SCOP | 1cne | ||||||||
| SUPERFAMILY | 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
- ↑ 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. doi:10.1016/s0969-2126(94)00082-4. PMID 7812715.
- ↑ 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.
- ↑ 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 incorporates text from the public domain Pfam and InterPro IPR008333
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