ID   NCPR_PHACH              Reviewed;         736 AA.
AC   Q9HDG2; Q9HG14;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
GN   Name=CPR;
OS   Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum
OS   pruinosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Homobasidiomycetes; Corticiales; Corticiaceae; Phanerochaete.
OX   NCBI_TaxID=5306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=ATCC 24725 / CBS 481.73 / CCRC 36200 / NRRL 6361 / VKM-F-1767;
RX   MEDLINE=20136378; PubMed=10672447; DOI=10.1007/s002940050010;
RA   Yadav J.S., Loper J.C.;
RT   "Cytochrome P450 oxidoreductase gene and its differentially terminated
RT   cDNAs from the white rot fungus Phanerochaete chrysosporium.";
RL   Curr. Genet. 37:65-73(2000).
RN   [2]
RP   KINETIC MECHANISM.
RX   MEDLINE=22325465; PubMed=12437968; DOI=10.1016/S0006-291X(02)02600-1;
RA   Warrilow A.G.S., Lamb D.C., Kelly D.E., Kelly S.L.;
RT   "Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic
RT   mechanism.";
RL   Biochem. Biophys. Res. Commun. 299:189-195(2002).
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 (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity).
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; AF193060; AAG31349.1; -; Genomic_DNA.
DR   EMBL; AF193061; AAG31350.1; -; mRNA.
DR   EMBL; AF193062; AAG31351.1; -; mRNA.
DR   HSSP; P00388; 1AMO.
DR   BRENDA; 1.6.2.4; 16698.
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; 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; Transmembrane.
FT   CHAIN         1    736       NADPH--cytochrome P450 reductase.
FT                                /FTId=PRO_0000167607.
FT   TRANSMEM      8     24       Potential.
FT   DOMAIN       66    216       Flavodoxin-like.
FT   DOMAIN      269    546       FAD-binding FR-type.
FT   NP_BIND     162    193       FMN (By similarity).
FT   NP_BIND     310    321       FAD (By similarity).
FT   NP_BIND     452    463       FAD (By similarity).
FT   NP_BIND     572    590       NADP (By similarity).
FT   NP_BIND     682    698       NADP (By similarity).
SQ   SEQUENCE   736 AA;  81628 MW;  AC45F12C96198AB1 CRC64;
     MAVSSSSDVI VLSVGIILAA LYLFREQIFS AAKPKTVQVP SSKAAAGGNG NPRDFIAKMK
     EGKKRIVIFY GSQTGTAEEY AIRLAKEAKS KFGLASLVCD PEEYDFENLD QVPEDCCVFF
     VMATYGEGEP TDNAVQLCQN LSDESFEFSN GEHKLPGLKY VIFGLGNKTY EHYNLISRNV
     DRDLQKMGAI RIGERGEGDD DKSMEEDYLE WKDGMWEAFA KAMNVEEGQG GDSPDFVVTE
     VFDHPEEKVY LGELSARALT RTKGIHDAKN PYPAPIIAAK ELFAPGSDRN CVHIELSTES
     SGITYQHGDH VGVWPSNADK EVDRLLYALG LHEKKDTVIN IESLDPALAK VPFPVPTTYA
     TVLRHYIDIS ALAGRQILGV LAKFAPNPEA EAVLKDLNSN KEHYQNIVAN GCMKLGEVLQ
     YAAGNDLHAD PTASNTTAWK IPFDIIVSSI PRLQPRYYSI SSSPKLYPNA IHATVVVLKY
     KSEKAPRVEE RWIYGVGSNF LLNLKYASHH DKAATLVSDD SPSEPSIVSH YPTYSIEGPR
     GAYKQGDVVK VPIHVRRSTF RLPTNPKSPV IMIGPGTGVA PFRGFVQERV AMARRTIEKH
     GPEGLADWGP IRLYYGCRRS DQDFLYKDEW PEYAKELHGK FIMRCAFSRE PPYKPDGSKI
     YVQDLIWEDA EQIADAILNG KGYVYICGDA KSMSKSVEET LCRILGEAKG GSAEVEGAAE
     LKLLKERNRL LLDVWS
//