[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8220474 [NCBI, ExPASy, EBI, Israel, Japan] Meijer A.H., Lopes Cardoso M.I., Voskuilen J.T., de Waal A., Verpoorte R., Hoge J.H.C.; "Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase, an enzyme essential for reactions catalysed by cytochrome P-450 mono-oxygenases in plants."; Plant J. 4:47-60(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. STRAIN=cv. Morning mist; Lopes Cardoso M.T., Meijer A.H., Rueb S., Queiroz Machado J., Memelink J., Hoge J.H.C.; Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
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.
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

X69791; CAA49446.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y09417; CAA70571.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S31502; S31502.

3D structure databases

HSSP

P00388; 1AMO. [HSSP ENTRY / PDB]

ModBase

Q05001.

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

Q05001.

Other

UniRef

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

Keywords

Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 714`	`714`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167610`
`DOMAIN`	`104 254`	`151`	`Flavodoxin-like.`
`DOMAIN`	`312 559`	`248`	`FAD-binding FR-type.`
`NP_BIND`	`200 231`	`32`	`FMN (By similarity).`
`NP_BIND`	`348 359`	`12`	`FAD (By similarity).`
`NP_BIND`	`489 499`	`11`	`FAD (By similarity).`
`NP_BIND`	`567 585`	`19`	`NADP (By similarity).`
`NP_BIND`	`661 677`	`17`	`NADP (By similarity).`

Sequence information

Length: 714 AA [This is the length of the unprocessed precursor]

Molecular weight: 78958 Da [This is the MW of the unprocessed precursor]

CRC64: DBDD9AF41374CF91 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDSSSEKLSP FELMSAILKG AKLDGSNSSD SGVAVSPAVM AMLLENKELV MILTTSVAVL 

        70         80         90        100        110        120 
IGCVVVLIWR RSSGSGKKVV EPPKLIVPKS VVEPEEIDEG KKKFTIFFGT QTGTAEGFAK 

       130        140        150        160        170        180 
ALAEEAKARY EKAVIKVIDI DDYAADDEEY EEKFRKETLA FFILATYGDG EPTDNAARFY 

       190        200        210        220        230        240 
KWFVEGNDRG DWLKNLQYGV FGLGNRQYEH FNKIAKVVDE KVAEQGGKRI VPLVLGDDDQ 

       250        260        270        280        290        300 
CIEDDFAAWR ENVWPELDNL LRDEDDTTVS TTYTAAIPEY RVVFPDKSDS LISEANGHAN 

       310        320        330        340        350        360 
GYANGNTVYD AQHPCRSNVA VRKELHTPAS DRSCTHLDFD IAGTGLSYGT GDHVGVYCDN 

       370        380        390        400        410        420 
LSETVEEAER LLNLPPETYF SLHADKEDGT PLAGSSLPPP FPPCTLRTAL TRYADLLNTP 

       430        440        450        460        470        480 
KKSALLALAA YASDPNEADR LKYLASPAGK DEYAQSLVAN QRSLLEVMAE FPSAKPPLGV 

       490        500        510        520        530        540 
FFAAIAPRLQ PRFYSISSSP RMAPSRIHVT CALVYEKTPG GRIHKGVCST WMKNAIPLEE 

       550        560        570        580        590        600 
SRDCSWAPIF VRQSNFKLPA DPKVPVIMIG PGTGLAPFRG FLQERLALKE EGAELGTAVF 

       610        620        630        640        650        660 
FFGCRNRKMD YIYEDELNHF LEIGALSELL VAFSREGPTK QYVQHKMAEK ASDIWRMISD 

       670        680        690        700        710 
GAYVYVCGDA KGMARDVHRT LHTIAQEQGS MDSTQAEGFV KNLQMTGRYL RDVW

Q05001 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