A0A9P5ZK47 · A0A9P5ZK47_PLEER
- ProteinNADPH--cytochrome P450 reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids732 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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. Involved in ergosterol biosynthesis.
Catalytic activity
- NADPH + 2 oxidized [cytochrome P450] = H+ + NADP+ + 2 reduced [cytochrome P450]
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per monomer.
Note: Binds 1 FMN per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 71-76 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SQTGTA | ||||||
Binding site | 122-125 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATYG | ||||||
Binding site | 164-173 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGNKTYEHYN | ||||||
Binding site | 199 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 455-458 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RYYS | ||||||
Binding site | 473-475 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TAV | ||||||
Binding site | 479 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 494-497 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVGS | ||||||
Binding site | 574 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 645-646 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 655-659 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KIYVQ | ||||||
Binding site | 731 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | plasma membrane | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | NADP binding | |
Molecular Function | NADPH-hemoprotein reductase activity | |
Biological Process | ergosterol biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH--cytochrome P450 reductase
- EC number
- Short namesCPR ; P450R
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Pleurotineae > Pleurotaceae > Pleurotus
Accessions
- Primary accessionA0A9P5ZK47
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass membrane protein
Mitochondrion outer membrane ; Single-pass membrane protein
Cell membrane ; Single-pass membrane protein
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 65-215 | Flavodoxin-like | ||||
Sequence: LVIFYGSQTGTAEEYAIRLAKEAKSKFGLASLVCDPEEYDFENLDQLPEDCAIFFVMATYGEGEPTDNAVTLMQNLEDESFEFSNGEHRLEGLKYVVFSLGNKTYEHYNKIGRDVDNVLTKMGAIRIGERGEGDDDKSMEEDYLEWKDGMW | ||||||
Domain | 268-543 | FAD-binding FR-type | ||||
Sequence: KNPFPAPISVARELFQSTHDRNCVHIELNTESSGISYQHGDHVGVWPSNPDVEVTRLLCALGLYEKKDNVIGIESLDPALAKVPFPVPTTYATVLRHYIDISAVAGRQILGALSKFAPNPEAEAFLKGLSTNKEEYHSLIANGCLKLGEVLQLAAGNDLSAAPTPENTTAWTIPFDIIVSSIPRLQPRYYSISSSPKLHPNSIHVTAVVLKYESIPNKRVNGRWIFGVGSNFLLNLKYAANEETAPLVATGSEFKAASVTIPGYAIEGPRGAYKQE |
Sequence similarities
Belongs to the NADPH--cytochrome P450 reductase family.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
In the N-terminal section; belongs to the flavodoxin family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length732
- Mass (Da)80,745
- Last updated2023-09-13 v1
- Checksum5BEE377727EBD9D5
Keywords
- Technical term