Q05001 (NCPR_CATRO) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: NADPH--cytochrome P450 reductase Short name=CPR Short name=P450R EC=1.6.2.4 | ||
| Gene names |
| ||
| Organism | Catharanthus roseus (Madagascar periwinkle) (Vinca rosea) | ||
| Taxonomic identifier | 4058 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Catharanthus![]() |
Protein attributes
| Sequence length | 714 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript 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; Peripheral membrane protein. Note: Anchored to the ER membrane by its N-terminal hydrophobic region. |
| 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 |
| Ligand | FAD FMN Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Cellular_component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activityInferred from electronic annotation. Source: EC 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 – 714 | 714 | NADPH--cytochrome P450 reductase | PRO_0000167610 | |||||
Regions | |||||||||
| Domain | 104 – 254 | 151 | Flavodoxin-like | ||||||
| Domain | 312 – 559 | 248 | FAD-binding FR-type | ||||||
| Nucleotide binding | 200 – 231 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 348 – 359 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 489 – 499 | 11 | FAD By similarity | ||||||
| Nucleotide binding | 567 – 585 | 19 | NADP By similarity | ||||||
| Nucleotide binding | 661 – 677 | 17 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase, an enzyme essential for reactions catalysed by cytochrome P-450 mono-oxygenases in plants." Meijer A.H., Lopes Cardoso M.I., Voskuilen J.T., de Waal A., Verpoorte R., Hoge J.H.C. Plant J. 4:47-60(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | Lopes Cardoso M.T., Meijer A.H., Rueb S., Queiroz Machado J., Memelink J., Hoge J.H.C. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. Strain: cv. Morning mist. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X69791 mRNA. Translation: CAA49446.1. Y09417 Genomic DNA. Translation: CAA70571.1. |
| PIR | S31502. |
3D structure databases | |
| ProteinModelPortal | Q05001. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 1.20.990.10. 1 hit. |
| InterPro | IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR001433. OxRdtase_FAD/NAD-bd. IPR023208. P450R. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view] |
| Pfam | PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PIRSF | PIRSF000208. P450R. 1 hit. |
| PRINTS | PR00369. FLAVODOXIN. PR00371. FPNCR. |
| SUPFAM | SSF63380. Riboflavin_synthase_like_b-brl. 1 hit. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NCPR_CATRO | ||||||||
| Accession | Primary (citable) accession number: Q05001 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
