Q653S9 · NCPR3_ORYSJ
- ProteinNADPH--cytochrome P450 reductase 3
- GeneCPR3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids714 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes (By similarity) (PubMed:23053415).
It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity).
It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity).
Catalytic activity
- NADPH + 2 oxidized [cytochrome P450] = H+ + NADP+ + 2 reduced [cytochrome P450]This reaction proceeds in the forward direction.
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 | 111-116 | FMN (UniProtKB | ChEBI) | ||||
Sequence: TQTGTA | ||||||
Binding site | 166-169 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATYG | ||||||
Binding site | 204-213 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGNRQYEHFN | ||||||
Binding site | 239 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 331 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 492-495 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RYYS | ||||||
Binding site | 510-512 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TCA | ||||||
Binding site | 526-529 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVCS | ||||||
Binding site | 573 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 634-635 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 640-644 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KEYVQ | ||||||
Binding site | 676 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 714 | 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 3
- EC number
- Short namesCPR ; P450R
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ653S9
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-44 | Lumenal | ||||
Sequence: MDSGGGGGGGALRPSALDLVAALLTGRGRPEEEGWPPSLAENRH | ||||||
Transmembrane | 45-65 | Helical | ||||
Sequence: LIVLLTTSLAVLVGCGVALLV | ||||||
Topological domain | 66-714 | Cytoplasmic | ||||
Sequence: RRSSISAPAVRAQEPQPRAPAPAKRKQEAEPDPDDGRQRVAVFFGTQTGTAEGFAKALAEEAKSRYDKAVFKVLDLDEYAADDEEYEQKLKKEIIALFFVATYGDGEPTDNAARFYKWFGEGNERGEWLSNLRFGVFGLGNRQYEHFNKVGKVVDQLLAEQGGKRIVPLGLGDDDQCIEDDFNAWKELLWPELDKLLRVEDDKSAAPTPYTAAIPEYRVVLVKPEEAMHINKSFSLSNGHAVYDIQHPCRANVAVRRELHTPASYRSCIHLEFDISGTGLTYETGDHVGVYAENCTETVEEVENLLGYSPDTLFSIHADQEDGTPLFGGSLPPPFPSPCTVGTALARYADLLSFPKKSALIALASHASDPKDAERLRHLASPAGKKEYSQWIVSSQRSLLEVMTEFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRMTPTRIHVTCALVYGQTPTGRIHKGVCSTWMKNSIPLEESQECSWAPIFVRQSNFKLPTDPTVPIIMIGPGTGLAPFRGFLQERLALKETGVELGHAVLFFGCRNRKMDFIYEDELNNFVETGALSELIVAFSREGPSKEYVQHKMAEKAPEIWSIISQGGYIYVCGDAKGMARDVHRTLHTIVQEQGSLDNSNTESYVKSLQMEGRYLRDVW |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000451430 | 1-714 | UniProt | NADPH--cytochrome P450 reductase 3 | |||
Sequence: MDSGGGGGGGALRPSALDLVAALLTGRGRPEEEGWPPSLAENRHLIVLLTTSLAVLVGCGVALLVRRSSISAPAVRAQEPQPRAPAPAKRKQEAEPDPDDGRQRVAVFFGTQTGTAEGFAKALAEEAKSRYDKAVFKVLDLDEYAADDEEYEQKLKKEIIALFFVATYGDGEPTDNAARFYKWFGEGNERGEWLSNLRFGVFGLGNRQYEHFNKVGKVVDQLLAEQGGKRIVPLGLGDDDQCIEDDFNAWKELLWPELDKLLRVEDDKSAAPTPYTAAIPEYRVVLVKPEEAMHINKSFSLSNGHAVYDIQHPCRANVAVRRELHTPASYRSCIHLEFDISGTGLTYETGDHVGVYAENCTETVEEVENLLGYSPDTLFSIHADQEDGTPLFGGSLPPPFPSPCTVGTALARYADLLSFPKKSALIALASHASDPKDAERLRHLASPAGKKEYSQWIVSSQRSLLEVMTEFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRMTPTRIHVTCALVYGQTPTGRIHKGVCSTWMKNSIPLEESQECSWAPIFVRQSNFKLPTDPTVPIIMIGPGTGLAPFRGFLQERLALKETGVELGHAVLFFGCRNRKMDFIYEDELNNFVETGALSELIVAFSREGPSKEYVQHKMAEKAPEIWSIISQGGYIYVCGDAKGMARDVHRTLHTIVQEQGSLDNSNTESYVKSLQMEGRYLRDVW | |||||||
Modified residue (large scale data) | 300 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 74-103 | Disordered | ||||
Sequence: AVRAQEPQPRAPAPAKRKQEAEPDPDDGRQ | ||||||
Compositional bias | 86-102 | Basic and acidic residues | ||||
Sequence: APAKRKQEAEPDPDDGR | ||||||
Domain | 105-255 | Flavodoxin-like | ||||
Sequence: VAVFFGTQTGTAEGFAKALAEEAKSRYDKAVFKVLDLDEYAADDEEYEQKLKKEIIALFFVATYGDGEPTDNAARFYKWFGEGNERGEWLSNLRFGVFGLGNRQYEHFNKVGKVVDQLLAEQGGKRIVPLGLGDDDQCIEDDFNAWKELLW | ||||||
Domain | 311-559 | FAD-binding FR-type | ||||
Sequence: QHPCRANVAVRRELHTPASYRSCIHLEFDISGTGLTYETGDHVGVYAENCTETVEEVENLLGYSPDTLFSIHADQEDGTPLFGGSLPPPFPSPCTVGTALARYADLLSFPKKSALIALASHASDPKDAERLRHLASPAGKKEYSQWIVSSQRSLLEVMTEFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRMTPTRIHVTCALVYGQTPTGRIHKGVCSTWMKNSIPLEESQECSWAPIFVRQSNFKLP |
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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length714
- Mass (Da)78,802
- Last updated2004-10-25 v1
- Checksum04F5C40ABEA9F8EB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 86-102 | Basic and acidic residues | ||||
Sequence: APAKRKQEAEPDPDDGR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP005090 EMBL· GenBank· DDBJ | BAD45947.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008215 EMBL· GenBank· DDBJ | BAF25828.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014965 EMBL· GenBank· DDBJ | BAT09381.1 EMBL· GenBank· DDBJ | Genomic DNA |