ID   CP51_ASHGO              Reviewed;         529 AA.
AC   Q759W0;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 33.
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=Lanosterol 14-alpha demethylase;
DE   AltName: Full=P450-14DM;
GN   Name=ERG11; Synonyms=CYP51; OrderedLocusNames=ADR162W;
OS   Ashbya gossypii (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=33169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
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; AE016817; AAS52083.1; -; Genomic_DNA.
DR   RefSeq; NP_984259.1; -.
DR   GeneID; 4620421; -.
DR   KEGG; ago:AGOS_ADR162W; -.
DR   NMPDR; fig|33169.1.peg.1904; -.
DR   AGD; ADR162W; -.
DR   HOGENOM; Q759W0; -.
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   3: Inferred from homology;
KW   Complete proteome; Heme; Iron; Lipid synthesis; Membrane;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW   Steroid biosynthesis; Sterol biosynthesis.
FT   CHAIN         1    529       Cytochrome P450 51.
FT                                /FTId=PRO_0000052002.
FT   METAL       468    468       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   529 AA;  60506 MW;  BE674CB09ABD67DA CRC64;
     MSESLLQTVV AYVELVLHHF MALSWTQQLS IVIVAPFIYS LVWQTLYSFR KDRVPLVPFM
     VPWVGSALAY GRAPYEFFGK CQQKYGDVFA FMLLGRVMTV YLGTKGHEFI LNAKLAEVSA
     EEAYTKLTTP VFGEGVVYDC PNHRLMEQKK FCKNALSTEA FRRYVPMVMD EVRKYLRTSK
     HFMMNERSSG VVNVMETQPE MTIFTASRSL LGAEMHSMLD ADFAYLYADL DKGFTPLNFV
     FRDLPLDNYR RRDNAQRTIS STYMKVIERR RKNNDVQDRD LIDALMTSAQ YKDGVKMTDQ
     QIANLLIGVL MGGQHTSAAT SAWVLLHLAE RPDIQEELYE EQMRVLDGGA KELTYELLQE
     MPLLNQVIKE TLRMHHPLHS LFRKVTRDMP VPNTSYVIPK DHYVLASPGF CHLSEEYFPN
     AKEFNPHRWD NDAASSVSTG EKVDYGFGAI SKGVSSPYLP FGGGRHRCIG EGFAYMQLGT
     IFSVVVRSMK WHFPADMKGV PNPDFTSMVT LPSEPCRIAW ERRVPDQII
//