A0A5B6UBJ4 · A0A5B6UBJ4_9ROSI
- ProteinNADPH--cytochrome P450 reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids673 (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.
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 | 91-96 | FMN (UniProtKB | ChEBI) | ||||
Sequence: TQTGTA | ||||||
Binding site | 126-129 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATYG | ||||||
Binding site | 164-173 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGNRQYEHFN | ||||||
Binding site | 199 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 451-454 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RYYS | ||||||
Binding site | 469-471 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TCA | ||||||
Binding site | 485-488 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVCS | ||||||
Binding site | 532 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 593-594 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 599-603 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KEYVQ | ||||||
Binding site | 635 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 673 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | NADP binding | |
Molecular Function | NADPH-hemoprotein reductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH--cytochrome P450 reductase
- EC number
- Short namesCPR ; P450R
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Malvales > Malvaceae > Malvoideae > Gossypium
Accessions
- Primary accessionA0A5B6UBJ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 27-46 | Helical | ||||
Sequence: MIVIATTSLAVILGLLVFFW |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 85-215 | Flavodoxin-like | ||||
Sequence: VTIFYGTQTGTAEGFAKDDYAMDDEQYEEKLKKETLAFFMVATYGDGEPTDNAARFYKWFTEGNERLPWLQQLTYGVFGLGNRQYEHFNKIAKVLDEQLSEQGAKRLIEVGLGDDDQCIEDDFTAWRELLW | ||||||
Domain | 271-518 | FAD-binding FR-type | ||||
Sequence: HHPCRVNVAVQRELHKPESDRSCIHLEFDISGTGITYETGDHVGVYADNCVETVEEAARLLGQPLDLLFSIHTDNEDGTSAGSSLPPPFASPCTLRMALARYADLLNPPRKAALIALAAHATEPSEAEKLKFLSSPQGKDEYSQWVVASQRSLLEVMAEFPSAKPPLGVFFAAVAPRLQPRYYSISSSPRFVPARVHVTCALVYGPTPTGRIHRGVCSTWMKNAVPLEKSNDCSWAPIFIRQSNFKLP |
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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length673
- Mass (Da)74,890
- Last updated2019-11-13 v1
- Checksum27E46BBE894B0332
Keywords
- Technical term