Q9SB48 · NCPR1_ARATH
- ProteinNADPH--cytochrome P450 reductase 1
- GeneATR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids692 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- NADPH + 2 oxidized [cytochrome P450] = H+ + NADP+ + 2 reduced [cytochrome P450]
Cofactor
Biotechnology
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.2 μM | NADPH | 7.0 | 25 | |||
21.9 μM | NADPH | 7.7 | 28 | |||
2 μM | NADPH | 7.25 | 25 | |||
17 μM | cytochrome c | 7.0 | 25 | |||
24.3 μM | cytochrome c | 7.7 | 28 |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 91-96 | FMN (UniProtKB | ChEBI) | ||||
Sequence: TQTGTA | ||||||
Binding site | 146-149 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATYG | ||||||
Binding site | 184-193 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGNRQYEHFN | ||||||
Binding site | 219 | FMN (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 310 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 470-473 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RYYS | ||||||
Binding site | 488-490 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TSA | ||||||
Binding site | 504-507 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVCS | ||||||
Binding site | 551 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 612-613 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 618-622 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KEYVQ | ||||||
Binding site | 654 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 692 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
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 | |
Biological Process | phenylpropanoid metabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH--cytochrome P450 reductase 1
- EC number
- Short namesAtCPR1 ; CPR 1 ; P450R 1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SB48
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-26 | Lumenal | ||||
Sequence: TSALYASDLFKQLKSIMGTDSLSDD | ||||||
Transmembrane | 27-47 | Helical | ||||
Sequence: VVLVIATTSLALVAGFVVLLW | ||||||
Topological domain | 48-692 | Cytoplasmic | ||||
Sequence: KKTTADRSGELKPLMIPKSLMAKDEDDDLDLGSGKTRVSIFFGTQTGTAEGFAKALSEEIKARYEKAAVKVIDLDDYAADDDQYEEKLKKETLAFFCVATYGDGEPTDNAARFYKWFTEENERDIKLQQLAYGVFALGNRQYEHFNKIGIVLDEELCKKGAKRLIEVGLGDDDQSIEDDFNAWKESLWSELDKLLKDEDDKSVATPYTAVIPEYRVVTHDPRFTTQKSMESNVANGNTTIDIHHPCRVDVAVQKELHTHESDRSCIHLEFDISRTGITYETGDHVGVYAENHVEIVEEAGKLLGHSLDLVFSIHADKEDGSPLESAVPPPFPGPCTLGTGLARYADLLNPPRKSALVALAAYATEPSEAEKLKHLTSPDGKDEYSQWIVASQRSLLEVMAAFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRLAPSRVHVTSALVYGPTPTGRIHKGVCSTWMKNAVPAEKSHECSGAPIFIRASNFKLPSNPSTPIVMVGPGTGLAPFRGFLQERMALKEDGEELGSSLLFFGCRNRQMDFIYEDELNNFVDQGVISELIMAFSREGAQKEYVQHKMMEKAAQVWDLIKEEGYLYVCGDAKGMARDVHRTLHTIVQEQEGVSSSEAEAIVKKLQTEGRYLRDVW |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 39 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylthreonine | ||||
Sequence: T | ||||||
Chain | PRO_0000416839 | 2-692 | NADPH--cytochrome P450 reductase 1 | |||
Sequence: TSALYASDLFKQLKSIMGTDSLSDDVVLVIATTSLALVAGFVVLLWKKTTADRSGELKPLMIPKSLMAKDEDDDLDLGSGKTRVSIFFGTQTGTAEGFAKALSEEIKARYEKAAVKVIDLDDYAADDDQYEEKLKKETLAFFCVATYGDGEPTDNAARFYKWFTEENERDIKLQQLAYGVFALGNRQYEHFNKIGIVLDEELCKKGAKRLIEVGLGDDDQSIEDDFNAWKESLWSELDKLLKDEDDKSVATPYTAVIPEYRVVTHDPRFTTQKSMESNVANGNTTIDIHHPCRVDVAVQKELHTHESDRSCIHLEFDISRTGITYETGDHVGVYAENHVEIVEEAGKLLGHSLDLVFSIHADKEDGSPLESAVPPPFPGPCTLGTGLARYADLLNPPRKSALVALAAYATEPSEAEKLKHLTSPDGKDEYSQWIVASQRSLLEVMAAFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRLAPSRVHVTSALVYGPTPTGRIHKGVCSTWMKNAVPAEKSHECSGAPIFIRASNFKLPSNPSTPIVMVGPGTGLAPFRGFLQERMALKEDGEELGSSLLFFGCRNRQMDFIYEDELNNFVDQGVISELIMAFSREGAQKEYVQHKMMEKAAQVWDLIKEEGYLYVCGDAKGMARDVHRTLHTIVQEQEGVSSSEAEAIVKKLQTEGRYLRDVW | ||||||
Modified residue | 249 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 85-235 | Flavodoxin-like | ||||
Sequence: VSIFFGTQTGTAEGFAKALSEEIKARYEKAAVKVIDLDDYAADDDQYEEKLKKETLAFFCVATYGDGEPTDNAARFYKWFTEENERDIKLQQLAYGVFALGNRQYEHFNKIGIVLDEELCKKGAKRLIEVGLGDDDQSIEDDFNAWKESLW | ||||||
Domain | 290-537 | FAD-binding FR-type | ||||
Sequence: HHPCRVDVAVQKELHTHESDRSCIHLEFDISRTGITYETGDHVGVYAENHVEIVEEAGKLLGHSLDLVFSIHADKEDGSPLESAVPPPFPGPCTLGTGLARYADLLNPPRKSALVALAAYATEPSEAEKLKHLTSPDGKDEYSQWIVASQRSLLEVMAAFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRLAPSRVHVTSALVYGPTPTGRIHKGVCSTWMKNAVPAEKSHECSGAPIFIRASNFKLP |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q9SB48-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length692
- Mass (Da)76,766
- Last updated2000-05-01 v1
- Checksum7DD77E418CCF2FA6
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JQY4 | F4JQY4_ARATH | ATR1 | 688 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 161 | in Ref. 1; CAA46814 | ||||
Sequence: Y → S | ||||||
Sequence conflict | 477-480 | in Ref. 1; CAA46814 | ||||
Sequence: SPRL → CQDW |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X66016 EMBL· GenBank· DDBJ | CAA46814.1 EMBL· GenBank· DDBJ | mRNA | ||
AL035356 EMBL· GenBank· DDBJ | CAA23011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161561 EMBL· GenBank· DDBJ | CAB79362.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE84919.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY054688 EMBL· GenBank· DDBJ | AAK96879.1 EMBL· GenBank· DDBJ | mRNA | ||
BT008426 EMBL· GenBank· DDBJ | AAP37785.1 EMBL· GenBank· DDBJ | mRNA |