Reviewed,
UniProtKB/Swiss-Prot Q00141 (NCPR_ASPNG)
Last modified
November 25, 2008.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADPH--cytochrome P450 reductase Short name=CPR Short name=P450R EC=1.6.2.4 | ||
| Gene names |
| ||
| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 693 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. |
| Catalytic activity | NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein. |
| Cofactor | FAD. FMN. |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass membrane proteinBy similarity. |
| Induction | By benzoic acid (BA). |
| Sequence similarities | In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane |
| Ligand | FAD FMN Flavoprotein NADP |
| Molecular function | Oxidoreductase |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Ref.1 Inferred from direct assay. Source: UniProtKB |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW microsome Ref.2Inferred from direct assay. Source: UniProtKB |
| Molecular function | FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activityInferred from electronic annotation. Source: EC electron carrier activity Ref.1Inferred from direct assay. Source: UniProtKB iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 693 | 693 | NADPH--cytochrome P450 reductase | PRO_0000167604 | |||||
Regions | |||||||||
| Transmembrane | 9 – 31 | 23 | Potential | ||||||
| Domain | 66 – 220 | 155 | Flavodoxin-like | ||||||
| Domain | 276 – 522 | 247 | FAD-binding FR-type | ||||||
| Nucleotide binding | 165 – 196 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 316 – 327 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 445 – 456 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 545 – 563 | 19 | NADP By similarity | ||||||
| Nucleotide binding | 640 – 656 | 17 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger." van den Brink H.J.M., van Zeijl C.M.J., Brons J.F., van den Hondel C.A.M.J.J., van Gorcom R.F.M. DNA Cell Biol. 14:719-729(1995) [PubMed: 7646819] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400. |
| [2] | "Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger." Faber B.W., van Gorcom R.F.M., Duine J.A. Arch. Biochem. Biophys. 394:245-254(2001) [PubMed: 11594739] [Abstract] Cited for: CHARACTERIZATION. Strain: T18.5. |
Cross-references
Sequence databases | |
|---|---|
| Z26938 Genomic DNA. Translation: CAA81550.1. | |
| PIR | S38427. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B1C based on UniProtKB P16435. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR003097. FAD-binding_1. IPR001094. Flavdoxin_like. IPR008254. Flavodoxin/NO_synth. IPR001709. FPN_cyt_redctse. IPR015702. NADPH_Cyt_Red. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] |
| PANTHER | PTHR19384:SF17. NADPH_Cyt_Red. 1 hit. |
| Pfam | PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00369. FLAVODOXIN. PR00371. FPNCR. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NCPR_ASPNG | ||||||||
| Accession | Primary (citable) accession number: Q00141 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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