ID   CP51_UNCNE              Reviewed;         524 AA.
AC   O14442; O14422;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   25-NOV-2008, entry version 52.
DE   RecName: Full=Cytochrome P450 51;
DE            EC=1.14.13.70;
DE   AltName: Full=CYPLI;
DE   AltName: Full=P450-LIA1;
DE   AltName: Full=Sterol 14-alpha demethylase;
DE   AltName: Full=Eburicol 14-alpha-demethylase;
DE   AltName: Full=P450-14DM;
GN   Name=CYP51;
OS   Uncinula necator (Grape powdery mildew).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=52586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT PHE-136.
RC   STRAIN=FPE11;
RX   MEDLINE=97444284; PubMed=9300816; DOI=10.1016/S0378-1119(97)00141-8;
RA   Delye C., Laigret F., Corio-Costet M.-F.;
RT   "Cloning and sequence analysis of the eburicol 14alpha-demethylase
RT   gene of the obligate biotrophic grape powdery mildew fungus.";
RL   Gene 195:29-33(1997).
RN   [2]
RP   SEQUENCE REVISION TO 515-517.
RA   Delye C., Laigret F., Corio-Costet M.-F.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   MOLECULAR BASIS OF FUNGICIDE RESISTANCE.
RC   STRAIN=PAZ11;
RX   MEDLINE=97394921; PubMed=9251183;
RA   Delye C., Laigret F., Corio-Costet M.-F.;
RT   "A mutation in the 14 alpha-demethylase gene of Uncinula necator that
RT   correlates with resistance to a sterol biosynthesis inhibitor.";
RL   Appl. Environ. Microbiol. 63:2966-2970(1997).
CC   -!- FUNCTION: Catalyzes C14-demethylation of lanosterol which is
CC       critical for ergosterol biosynthesis. It transforms lanosterol
CC       into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-
CC       methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3
CC       NADP(+) + 4 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Membrane (Potential). Membrane; Single-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U72657; AAC49811.2; -; Genomic_DNA.
DR   EMBL; U72658; AAC49812.2; -; mRNA.
DR   EMBL; U83840; AAC49801.2; -; Genomic_DNA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Lipid synthesis; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis.
FT   CHAIN         1    524       Cytochrome P450 51.
FT                                /FTId=PRO_0000052010.
FT   METAL       469    469       Iron (heme axial ligand) (By similarity).
FT   VARIANT     136    136       Y -> F (in strain: PAZ11; resistant to
FT                                triadimenol; a sterol demethylation-
FT                                inhibiting fungicide).
SQ   SEQUENCE   524 AA;  59840 MW;  24BE154B176CE09A CRC64;
     MYIADILSDL LTQQTTRYGW IFMVTSIAFS IILLAVGLNV LSQLLFRRPY EPPVVFHWFP
     IIGSTISYGI DPYKFYFDCR AKYGDIFTFI LLGKKVTVYL GLQGNNFILN GKLKDVNAEE
     IYTNLTTPVF GRDVVYDCPN SKLMEQKKFM KTALTIEAFH SYVTIIQNEV EAYINNCVSF
     QGESGTVNIS KVMAEITIYT ASHALQGEEV RENFDSSFAA LYHDLDMGFT PINFTFYWAP
     LPWNRARDHA QRTVARTYMN IIQARREEKR SGENKHDIMW ELMRSTYKDG TPVPDREIAH
     MMIALLMAGQ HSSSSTSSWI MLWLAARPDI MEELYEEQLR IFGSEKPFPP LQYEDLSKLQ
     LHQNVLKEVL RLHAPIHSIM RKVKNPMIVP GTKYVIPTSH VLISSPGCTS QDATFFPDPL
     KWDPHRWDIG SGKVLGNDAV DEKYDYGYGL TSTGASSPYL PFGAGRHRCI GEQFATLQLV
     TIMATMVRFF RFRNIDGKQG VVKTDYSSLF SMPLAPALIG WEKR
//