ID   NCPR_CATRO              Reviewed;         714 AA.
AC   Q05001;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
GN   Name=CPR;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94035173; PubMed=8220474;
RX   DOI=10.1046/j.1365-313X.1993.04010047.x;
RA   Meijer A.H., Lopes Cardoso M.I., Voskuilen J.T., de Waal A.,
RA   Verpoorte R., Hoge J.H.C.;
RT   "Isolation and characterization of a cDNA clone from Catharanthus
RT   roseus encoding NADPH:cytochrome P-450 reductase, an enzyme essential
RT   for reactions catalysed by cytochrome P-450 mono-oxygenases in
RT   plants.";
RL   Plant J. 4:47-60(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC   STRAIN=cv. Morning mist;
RA   Lopes Cardoso M.T., Meijer A.H., Rueb S., Queiroz Machado J.,
RA   Memelink J., Hoge J.H.C.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP
CC       to cytochrome P450 in microsomes. It can also provide electron
CC       transfer to heme oxygenase and cytochrome B5.
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: FMN.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Note=Anchored to the ER membrane by its N-
CC       terminal hydrophobic region.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X69791; CAA49446.1; -; mRNA.
DR   EMBL; Y09417; CAA70571.1; -; Genomic_DNA.
DR   PIR; S31502; S31502.
DR   HSSP; P00388; 1AMO.
DR   BRENDA; 1.6.2.4; 20471.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR015702; NADPH_Cyt_P450_Rdtase.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   PANTHER; PTHR19384:SF17; NADPH_Cyt_Red; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    714       NADPH--cytochrome P450 reductase.
FT                                /FTId=PRO_0000167610.
FT   DOMAIN      104    254       Flavodoxin-like.
FT   DOMAIN      312    559       FAD-binding FR-type.
FT   NP_BIND     200    231       FMN (By similarity).
FT   NP_BIND     348    359       FAD (By similarity).
FT   NP_BIND     489    499       FAD (By similarity).
FT   NP_BIND     567    585       NADP (By similarity).
FT   NP_BIND     661    677       NADP (By similarity).
SQ   SEQUENCE   714 AA;  78958 MW;  DBDD9AF41374CF91 CRC64;
     MDSSSEKLSP FELMSAILKG AKLDGSNSSD SGVAVSPAVM AMLLENKELV MILTTSVAVL
     IGCVVVLIWR RSSGSGKKVV EPPKLIVPKS VVEPEEIDEG KKKFTIFFGT QTGTAEGFAK
     ALAEEAKARY EKAVIKVIDI DDYAADDEEY EEKFRKETLA FFILATYGDG EPTDNAARFY
     KWFVEGNDRG DWLKNLQYGV FGLGNRQYEH FNKIAKVVDE KVAEQGGKRI VPLVLGDDDQ
     CIEDDFAAWR ENVWPELDNL LRDEDDTTVS TTYTAAIPEY RVVFPDKSDS LISEANGHAN
     GYANGNTVYD AQHPCRSNVA VRKELHTPAS DRSCTHLDFD IAGTGLSYGT GDHVGVYCDN
     LSETVEEAER LLNLPPETYF SLHADKEDGT PLAGSSLPPP FPPCTLRTAL TRYADLLNTP
     KKSALLALAA YASDPNEADR LKYLASPAGK DEYAQSLVAN QRSLLEVMAE FPSAKPPLGV
     FFAAIAPRLQ PRFYSISSSP RMAPSRIHVT CALVYEKTPG GRIHKGVCST WMKNAIPLEE
     SRDCSWAPIF VRQSNFKLPA DPKVPVIMIG PGTGLAPFRG FLQERLALKE EGAELGTAVF
     FFGCRNRKMD YIYEDELNHF LEIGALSELL VAFSREGPTK QYVQHKMAEK ASDIWRMISD
     GAYVYVCGDA KGMARDVHRT LHTIAQEQGS MDSTQAEGFV KNLQMTGRYL RDVW
//