A0A2H5BXD1 · A0A2H5BXD1_GLYUR
- ProteinNADPH--cytochrome P450 reductase
- GeneCPR1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids691 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 88-93 | FMN (UniProtKB | ChEBI) | ||||
Sequence: TQTGTA | ||||||
Binding site | 143-146 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATYG | ||||||
Binding site | 182-191 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGNKQYEHFN | ||||||
Binding site | 217 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 309 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 469-472 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RYYS | ||||||
Binding site | 487-489 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TCA | ||||||
Binding site | 503-506 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVCS | ||||||
Binding site | 550 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 611-612 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 617-621 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KEYVQ | ||||||
Binding site | 653 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 691 | 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
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Galegeae > Glycyrrhiza
Accessions
- Primary accessionA0A2H5BXD1
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: LVLIATTSVAVIIGLLVFLW |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 82-233 | Flavodoxin-like | ||||
Sequence: VTVFFGTQTGTAEGFAKALADEIKARYEKAYVKVVDLDDYAMDDDQYEEKLKKETLAFFMLATYGDGEPTDNAARFYKWFTEGKEERGTWLQQLTHGVFGLGNKQYEHFNKIGKVVDEDLSEQGAKRLVPLGLGDDDQSIEDDFSAWKESLW | ||||||
Domain | 289-536 | FAD-binding FR-type | ||||
Sequence: HHPCRVNVAVKRELHKPQSDRSCIHLEFDISGTGITYETGDHVGVYAENCDETVEEAGKLLGQNLDLLFSLHTDNEDGTSLGGSLLPPFPGPCTLRTALARYADLLNPPRKAALVVLAAHASEPSEAERLKFLSSPQGKDEYSKWVVGSQRSLLEVMAEFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRFASQRVHVTCALVYGPTPTGRIHKGVCSTWMKNAIPLEESRDCGWAPIFIRPSNFKLP |
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
- Length691
- Mass (Da)76,810
- Last updated2018-02-28 v1
- Checksum220034423CD34543