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Protein

NADPH--cytochrome P450 reductase

Gene
N/A
Organism
Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 21032FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi325 – 33612FADBy similarityAdd
BLAST
Nucleotide bindingi465 – 47511FADBy similarityAdd
BLAST
Nucleotide bindingi544 – 56219NADPBy similarityAdd
BLAST
Nucleotide bindingi639 – 65416NADPBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Short name:
CPR
Short name:
P450R
OrganismiVigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Taxonomic identifieri3916 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690NADPH--cytochrome P450 reductasePRO_0000167611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP37116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 233152Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini289 – 535247FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNSDLVRA VESFLGVSLG DSVSDSLLLI ATTSAAVVVG LLVFLWKKSS
60 70 80 90 100
DRSKEVKPVV VPRDLMMEEE EEVDVAAGKT KVTIFFGTQT GTAEGFAKAL
110 120 130 140 150
AEEIKARYEK AAVKVVDLDD YAADDDLYEE KLKKESLVFF MLATYGDGEP
160 170 180 190 200
IDNAARFYKW FTEGKDERGI WLQKLTYGVF GLGNRQYEHF NKIGKVVDEE
210 220 230 240 250
LAEQGAKRLV AVGLGDDDQS IEDDFSAWKE SLWSELDQLL RDEDDANTVS
260 270 280 290 300
TPYTAAILEY RVVIHDPTAA STYDNHSTVA NGNTEFDIHH PCRVNVAVQK
310 320 330 340 350
ELHKPESDRS CIHLEFDISG TSITYDTGDH VGVYAENCNE TVEETGKLLG
360 370 380 390 400
QNLDLFFSLH TDKDDGTSLG GSLLPPFPGP CSLRTALARY ADLLNPPRKA
410 420 430 440 450
ALLALATHAS EPSDERLKFL SSPQGKDEYS KWVVGSQRSL VEVMAEFPSA
460 470 480 490 500
KPPLGVFFAA IAPRLQPRYY SISSSPRFAP QRVHVTCALV YGPTPTGRIH
510 520 530 540 550
KGVCSTWMKN AIPSEKSQDC SSAPIFIRPS NFKLPVDHSI PIIMVGPGTG
560 570 580 590 600
LAPFRGFLQE RYALKEDGVQ LGPALLFFGC RNRQMDFIYE DELKSFVEQG
610 620 630 640 650
SLSELIVAFS REGAEKEYVQ HKMMDKAAHL WSLISQGGYL YVCGDAKGMA
660 670 680 690
RDVHRTLHSI VQEQENVDST KAEAIVKKLQ MDGRYLRDVW
Length:690
Mass (Da):76,506
Last modified:October 1, 1994 - v1
Checksum:i592966167E8561DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07843 mRNA. Translation: AAA34240.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07843 mRNA. Translation: AAA34240.1.

3D structure databases

ProteinModelPortaliP37116.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Berken.
    Tissue: Seedling.

Entry informationi

Entry nameiNCPR_VIGRR
AccessioniPrimary (citable) accession number: P37116
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.