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Reviewed, UniProtKB/Swiss-Prot P37116 (NCPR_PHAAU)

Last modified October 13, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADPH--cytochrome P450 reductase
      Short name=CPR
      Short name=P450R
    EC=1.6.2.4
OrganismPhaseolus aureus (Mung bean) (Vigna radiata)
Taxonomic identifier3916 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IFabalesFabaceaePapilionoideaePhaseoleaeVigna

Protein attributes

Sequence length690 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This enzyme is required for electron transfer from NADP to cytochrome P450.

Catalytic activity

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

Cofactor

FAD.

FMN.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Note: Anchored to the ER membrane by its N-terminal hydrophobic region.

Post-translational modification

Glycosylated.

Sequence similarities

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 690690NADPH--cytochrome P450 reductase
PRO_0000167611

Regions

Domain82 – 233152Flavodoxin-like
Domain289 – 535247FAD-binding FR-type
Nucleotide binding179 – 21032FMN By similarity
Nucleotide binding325 – 33612FAD By similarity
Nucleotide binding465 – 47511FAD By similarity
Nucleotide binding544 – 56219NADP By similarity
Nucleotide binding639 – 65416NADP By similarity

Amino acid modifications

Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P37116-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 592966167E8561DE

FASTA69076,506
        10         20         30         40         50         60 
MASNSDLVRA VESFLGVSLG DSVSDSLLLI ATTSAAVVVG LLVFLWKKSS DRSKEVKPVV 

        70         80         90        100        110        120 
VPRDLMMEEE EEVDVAAGKT KVTIFFGTQT GTAEGFAKAL AEEIKARYEK AAVKVVDLDD 

       130        140        150        160        170        180 
YAADDDLYEE KLKKESLVFF MLATYGDGEP IDNAARFYKW FTEGKDERGI WLQKLTYGVF 

       190        200        210        220        230        240 
GLGNRQYEHF NKIGKVVDEE LAEQGAKRLV AVGLGDDDQS IEDDFSAWKE SLWSELDQLL 

       250        260        270        280        290        300 
RDEDDANTVS TPYTAAILEY RVVIHDPTAA STYDNHSTVA NGNTEFDIHH PCRVNVAVQK 

       310        320        330        340        350        360 
ELHKPESDRS CIHLEFDISG TSITYDTGDH VGVYAENCNE TVEETGKLLG QNLDLFFSLH 

       370        380        390        400        410        420 
TDKDDGTSLG GSLLPPFPGP CSLRTALARY ADLLNPPRKA ALLALATHAS EPSDERLKFL 

       430        440        450        460        470        480 
SSPQGKDEYS KWVVGSQRSL VEVMAEFPSA KPPLGVFFAA IAPRLQPRYY SISSSPRFAP 

       490        500        510        520        530        540 
QRVHVTCALV YGPTPTGRIH KGVCSTWMKN AIPSEKSQDC SSAPIFIRPS NFKLPVDHSI 

       550        560        570        580        590        600 
PIIMVGPGTG LAPFRGFLQE RYALKEDGVQ LGPALLFFGC RNRQMDFIYE DELKSFVEQG 

       610        620        630        640        650        660 
SLSELIVAFS REGAEKEYVQ HKMMDKAAHL WSLISQGGYL YVCGDAKGMA RDVHRTLHSI 

       670        680        690 
VQEQENVDST KAEAIVKKLQ MDGRYLRDVW 

« Hide

References

[1]"Purification, characterization, and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean."
Shet M.S., Sathasivan K., Arlotto M.A., Mehdy M.C., Estabrook R.W.
Proc. Natl. Acad. Sci. U.S.A. 90:2890-2894(1993) [PubMed: 8464904] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Berken.
Tissue: Seedling.

Cross-references

Sequence databases

L07843 mRNA. Translation: AAA34240.1.

3D structure databases

HSSPHSSP built from PDB template 1AMO based on UniProtKB P00388.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.6.2.4. 29.

Family and domain databases

InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015702. NADPH_Cyt_P450_Rdtase.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PANTHERPTHR19384:SF17. NADPH_Cyt_Red. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCPR_PHAAU
AccessionPrimary (citable) accession number: P37116
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 13, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents