NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. Berken;
TISSUE=Seedling;
PubMed=8464904 [NCBI, ExPASy, EBI, Israel, Japan]
Shet M.S., Sathasivan K., Arlotto M.A., Mehdy M.C., Estabrook R.W.;
"Purification, characterization, and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean.";
Proc. Natl. Acad. Sci. U.S.A. 90:2890-2894(1993).

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.
COFACTOR: FMN.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Anchored to the ER membrane by its N-terminal hydrophobic region.
PTM: Glycosylated.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L07843; AAA34240.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00388; 1AMO. [HSSP ENTRY / PDB]

ModBase

P37116.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0003958;	Molecular function: NADPH-hemoprotein reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

PANTHER

PTHR19384:SF17; NADPH_Cyt_Red; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P37116.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Glycoprotein; Membrane; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 690`	`690`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167611`
`DOMAIN`	`82 233`	`152`	`Flavodoxin-like.`
`DOMAIN`	`289 535`	`247`	`FAD-binding FR-type.`
`NP_BIND`	`179 210`	`32`	`FMN (By similarity).`
`NP_BIND`	`325 336`	`12`	`FAD (By similarity).`
`NP_BIND`	`465 475`	`11`	`FAD (By similarity).`
`NP_BIND`	`544 562`	`19`	`NADP (By similarity).`
`NP_BIND`	`639 654`	`16`	`NADP (By similarity).`
`CARBOHYD`	`275 275`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`339 339`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 690 AA [This is the length of the unprocessed precursor]

Molecular weight: 76506 Da [This is the MW of the unprocessed precursor]

CRC64: 592966167E8561DE [This is a checksum on the sequence]

        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

P37116 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools