P37201 (NCPR_CANTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
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 |
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| Organism | Candida tropicalis (Yeast) | ||||
| Taxonomic identifier | 5482 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida![]() |
Protein attributes
| Sequence length | 680 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 protein. |
| 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 Transmembrane helix |
| Ligand | FAD FMN Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Cellular_component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 680 | 680 | NADPH--cytochrome P450 reductase | PRO_0000167606 | |||||
Regions | |||||||||
| Transmembrane | 8 – 24 | 17 | Helical; Potential | ||||||
| Domain | 60 – 204 | 145 | Flavodoxin-like | ||||||
| Domain | 264 – 509 | 246 | FAD-binding FR-type | ||||||
| Nucleotide binding | 149 – 180 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 304 – 315 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 435 – 446 | 12 | FAD By similarity | ||||||
| Nucleotide binding | 532 – 550 | 19 | NADP By similarity | ||||||
| Nucleotide binding | 628 – 644 | 17 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Isolation and characterization of the alkane-inducible NADPH-cytochrome P-450 oxidoreductase gene from Candida tropicalis. Identification of invariant residues within similar amino acid sequences of divergent flavoproteins." Sutter T.R., Sanglard D., Loper J.C. J. Biol. Chem. 265:16428-16436(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400. |
| [2] | Erratum Sutter T.R., Sanglard D., Loper J.C. J. Biol. Chem. 265:22056-22056(1990) |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M35199 Genomic DNA. Translation: AAA34333.1. |
| PIR | A37890. |
3D structure databases | |
| ProteinModelPortal | P37201. |
| SMR | P37201. Positions 46-680. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| SABIO-RK | P37201. |
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_CANTR | ||||||||
| Accession | Primary (citable) accession number: P37201 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
