Biology:Oxidoreductase FAD-binding domain
| Oxidoreductase FAD-binding domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | FAD_binding_6 | ||||||||||
| Pfam | PF00970 | ||||||||||
| InterPro | IPR008333 | ||||||||||
| SCOP2 | 1cne / SCOPe / SUPFAM | ||||||||||
| CDD | cd00322 | ||||||||||
| |||||||||||
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 include:
- CYB5R1; CYB5R2; CYB5R4; CYB5RL;
References
- ↑ "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. 1994. doi:10.1016/s0969-2126(94)00082-4. PMID 7812715.
- ↑ "Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution". Biochemistry 34 (9): 2763–2767. 1995. doi:10.1021/bi00009a004. PMID 7893687.
- ↑ "Structure-function relations for ferredoxin reductase". J. Bioenerg. Biomembr. 26 (1): 89–99. 1994. doi:10.1007/BF00763221. PMID 8027025.
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