ID   C505_FUSOX              Reviewed;        1066 AA.
AC   Q9Y8G7;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Bifunctional P-450:NADPH-P450 reductase;
DE   AltName: Full=Fatty acid omega-hydroxylase;
DE   AltName: Full=P450foxy;
DE   Includes:
DE     RecName: Full=Cytochrome P450 505;
DE              EC=1.14.14.1;
DE   Includes:
DE     RecName: Full=NADPH--cytochrome P450 reductase;
DE              EC=1.6.2.4;
GN   Name=CYP505;
OS   Fusarium oxysporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales;
OC   mitosporic Hypocreales; Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-99; 353-359;
RP   362-380; 518-538; 616-626 AND 1005-1009, AND SUBCELLULAR LOCATION.
RC   STRAIN=MT-811;
RX   MEDLINE=20564350; PubMed=10995755; DOI=10.1074/jbc.M005617200;
RA   Kitazume T., Takaya N., Nakayama N., Shoun H.;
RT   "Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a
RT   membrane-bound eukaryotic counterpart of Bacillus megaterium
RT   cytochrome P450BM3.";
RL   J. Biol. Chem. 275:39734-39740(2000).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=MT-811;
RX   MEDLINE=96271003; PubMed=8830036;
RA   Nakayama N., Takemae A., Shoun H.;
RT   "Cytochrome P450foxy, a catalytically self-sufficient fatty acid
RT   hydroxylase of the fungus Fusarium oxysporum.";
RL   J. Biochem. 119:435-440(1996).
CC   -!- FUNCTION: Functions as a fatty acid monooxygenase. Shows highest
CC       activity toward fatty acids with a chain length of 12-14 carbons.
CC       The reductase domain is required for electron transfer from NADP
CC       to cytochrome P450.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein.
CC   -!- COFACTOR: Binds 1 FAD (By similarity).
CC   -!- COFACTOR: Binds 1 FMN (By similarity).
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome
CC       P450 family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AB030037; BAA82526.1; -; Genomic_DNA.
DR   HSSP; P14779; 1JPZ.
DR   BRENDA; 1.14.14.1; 15244.
DR   BRENDA; 1.6.2.4; 15244.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR015702; NADPH_Cyt_P450_Rdtase.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; FAD; Flavoprotein; FMN;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Multifunctional enzyme; NADP; Oxidoreductase; Transport.
FT   CHAIN         1   1066       Bifunctional P-450:NADPH-P450 reductase.
FT                                /FTId=PRO_0000052210.
FT   DOMAIN      500    641       Flavodoxin-like.
FT   DOMAIN      676    904       FAD-binding FR-type.
FT   REGION        1    480       Cytochrome P450.
FT   REGION      481   1066       NADPH-P-450 reductase.
FT   METAL       407    407       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   1066 AA;  117926 MW;  6B8123698C223DBA CRC64;
     MAESVPIPEP PGYPLIGNLG EFTSNPLSDL NRLADTYGPI FRLRLGAKAP IFVSSNSLIN
     EVCDEKRFKK TLKSVLSQVR EGVHDGLFTA FEDEPNWGKA HRILVPAFGP LSIRGMFPEM
     HDIATQLCMK FARHGPRTPI DTSDNFTRLA LDTLALCAMD FRFYSYYKEE LHPFIEAMGD
     FLTESGNRNR RPPFAPNFLY RAANEKFYGD IALMKSVADE VVAARKASPS DRKDLLAAML
     NGVDPQTGEK LSDENITNQL ITFLIAGHET TSGTLSFAMY QLLKNPEAYS KVQKEVDEVV
     GRGPVLVEHL TKLPYISAVL RETLRLNSPI TAFGLEAIDD TFLGGKYLVK KGEIVTALLS
     RGHVDPVVYG NDADKFIPER MLDDEFARLN KEYPNCWKPF GNGKRACIGR PFAWQESLLA
     MVVLFQNFNF TMTDPNYALE IKQTLTIKPD HFYINATLRH GMTPTELEHV LAGNGATSSS
     THNIKAAANL DAKAGSGKPM AIFYGSNSGT CEALANRLAS DAPSHGFSAT TVGPLDQAKQ
     NLPEDRPVVI VTASYEGQPP SNAAHFIKWM EDLDGNDMEK VSYAVFACGH HDWVETFHRI
     PKLVDSTLEK RGGTRLVPMG SADAATSDMF SDFEAWEDIV LWPGLKEKYK ISDEESGGQK
     GLLVEVSTPR KTSLRQDVEE ALVVAEKTLT KSGPAKKHIE IQLPSAMTYK AGDYLAILPL
     NPKSTVARVF RRFSLAWDSF LKIQSEGPTT LPTNVAISAF DVFSAYVELS QPATKRNILA
     LAEATEDKDT IQELERLAGD AYQAEISPKR VSVLDLLEKF PAVALPISSY LAMLPPMRVR
     QYSISSSPFA DPSKLTLTYS LLDAPSLSGQ GRHVGVATNF LSHLTAGDKL HVSVRASSEA
     FHLPSDAEKT PIICVAAGTG LAPLRGFIQE RAAMLAAGRT LAPALLFFGC RNPEIDDLYA
     EEFERWEKMG AVDVRRAYSR ATDKSEGCKY VQDRVYHDRA DVFKVWDQGA KVFICGSREI
     GKAVEDVCVR LAIEKAQQNG RDVTEEMARA WFERSRNERF ATDVFD
//