ID   NCPR_CANMA              Reviewed;         680 AA.
AC   P50126;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 62.
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
GN   Name=NCP1;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=EH15D;
RX   MEDLINE=96267759; PubMed=8701606;
RX   DOI=10.1002/(SICI)1097-0061(19960330)12:4<333::AID-YEA915>3.3.CO;2-3;
RA   Kaergel E., Honeck H., Vogel F., Boehmer A., Schunk W.-H.;
RT   "Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-
RT   length cDNA, heterologous expression in Saccharomyces cerevisiae and
RT   function of the N-terminal region for membrane anchoring and
RT   proliferation of the endoplasmic reticulum.";
RL   Yeast 12:333-348(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / IFO 1977 / JCM 1504;
RX   MEDLINE=95400011; PubMed=7545482;
RA   Ohkuma M., Masuda Y., Park S.M., Ohtomo R., Ohta A., Takagi M.;
RT   "Evidence that the expression of the gene for NADPH-cytochrome P-450
RT   reductase is n-alkane-inducible in Candida maltosa.";
RL   Biosci. Biotechnol. Biochem. 59:1328-1330(1995).
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; Single-pass
CC       membrane protein.
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; X76226; CAA53812.1; -; mRNA.
DR   EMBL; D25327; BAA04997.1; -; Genomic_DNA.
DR   PIR; S63698; S63698.
DR   PIR; S63895; S63895.
DR   HSSP; P00388; 1AMO.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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; IPR001094; Flavdoxin_like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR015702; NADPH_Cyt_Red.
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; Transmembrane.
FT   CHAIN         1    680       NADPH--cytochrome P450 reductase.
FT                                /FTId=PRO_0000167605.
FT   TRANSMEM      8     24       Potential.
FT   DOMAIN       60    204       Flavodoxin-like.
FT   DOMAIN      264    509       FAD-binding FR-type.
FT   NP_BIND     149    180       FMN (By similarity).
FT   NP_BIND     304    315       FAD (By similarity).
FT   NP_BIND     435    446       FAD (By similarity).
FT   NP_BIND     532    550       NADP (By similarity).
FT   NP_BIND     628    644       NADP (By similarity).
FT   CONFLICT     30     30       Q -> E (in Ref. 2; BAA04997).
FT   CONFLICT    170    171       LL -> VF (in Ref. 2; BAA04997).
FT   CONFLICT    565    565       F -> P (in Ref. 2; BAA04997).
FT   CONFLICT    579    579       Q -> K (in Ref. 2; BAA04997).
FT   CONFLICT    619    619       V -> L (in Ref. 2; BAA04997).
FT   CONFLICT    664    664       E -> D (in Ref. 2; BAA04997).
SQ   SEQUENCE   680 AA;  77131 MW;  E396F81E169705C9 CRC64;
     MALDKLDLYV IIVLAVAVAA YFAKNQFLDQ PQDTGFLSND TAGGNSRDIL ETLKKNNKNT
     LLLFGSQTGT AEDYANKLSR EIHSRFGLKT MVADFADYDW DNFGDIPNDI LVFFIVATYG
     EGEPTDNADE FHTWLTDEAD TLSTLRYTVF GLGNSTYEFY NAIGRKFDRL LEEKGGERFA
     DYGEGDDGTG TLDEDFLTWK DNVFDTLKND LNFEERELKY EPNVKLTERD DLTVDDSEVS
     LGEPNKKYIQ SEEIDLTKGP FDHTHPYLAK ISKTRELFAS KERNCVHVEF DVSESNLKYT
     TGDHLAVWPS NSDENIAKFI KCFGLDDKIN TVFELKALDS TYQIPFPNPI TYGAVVRHHL
     EISGPVSRQF FLAIAGFAPD EETKKTFTRI GNDKQEFANK ITRKKLNVAD ALLFASNGRP
     WSDVPFEFII ENVPHLQPRY YSISSSSLSE KQTINITAVV EVEEEADGRA VTGVVTNLLK
     NIEIEQNKTG EKPVVHYDLS GPRNKFNKFK LPVHVRRSNF KLPKNTTTPV ILIGPGTGVA
     PLRGFVRERV QQVKNGVNVG KTVLFYGCRN EHDDFLYKQE WSEYASVLGE NFEMFTAFSR
     QDPSKKVYVQ DKIAENSKVV NDLLNEGAII YVCGDASRMA RDVQSTIAKI VAKHREIQED
     KAVELVKSWK VQNRYQEDVW
//