CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.80 | Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module |
Domain Context
CATH Clusters
Superfamily | Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module |
Functional Family | Bifunctional cytochrome P450/NADPH--P450 reductase |
Enzyme Information
1.6.2.4 |
NADPH--hemoprotein reductase.
based on mapping to UniProt P14779
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein.
-!- This enzyme catalyzes the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P450 monooxygenases (e.g. EC 1.14.14.1) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN. -!- It also reduces cytochrome b5 and cytochrome c. -!- The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
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1.14.14.1 |
Unspecific monooxygenase.
based on mapping to UniProt P14779
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. -!- Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH. -!- Some of the reactions attributed to EC 1.14.15.3 belong here. -!- Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1.
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UniProtKB Entries (1)
P14779 |
CPXB_BACMB
Bacillus megaterium NBRC 15308 = ATCC 14581
Bifunctional cytochrome P450/NADPH--P450 reductase
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PDB Structure
PDB | 4DQL |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3.
Febs J.
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