ID   CP51_CUNEL              Reviewed;         512 AA.
AC   Q9UVC3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   04-NOV-2008, entry version 43.
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=CYP51;
OS   Cunninghamella elegans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Basal fungal lineages;
OC   Mucoromycotina; Mucorales; Cunninghamellaceae; Cunninghamella.
OX   NCBI_TaxID=4853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 36112 / DSM 8217;
RA   Craft D.L., Loper J.C.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; AF046863; AAF20263.1; -; Genomic_DNA.
DR   HSSP; P77901; 1E9X.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Heme; Iron; Lipid synthesis; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis.
FT   CHAIN         1    512       Cytochrome P450 51.
FT                                /FTId=PRO_0000052006.
FT   METAL       458    458       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   512 AA;  57677 MW;  5E10C9D415CA15B1 CRC64;
     MAIVSQISRF ITFTIISMGY SVLAVGVALT IHILSQLIVP KNPNEPPNVF SLIPVLGNAV
     QFGMNPVAFL QECQKKYGDV FTFTMVGKRV TVCLGADGNQ FVFNSKQNLS SAAEAYNHMT
     KYVFGPDVVY DAPHAVFMEQ KKFIKAGLNS DCFRQHVPMI VQETEEFFKK FNKPTGFIEA
     YETFGSLIIY TASRCLMGKE IRASLDGNVA KLYYDLDQGF KPINFIFPNL PLPSYRRRDV
     ACKKMADLYS SIIQRRKDEK DNNNADLLQA LMDATYKDGT HIPDHHIAGM MIAVLFGGQH
     TSATTSAWTI LELANRPDII KALREEQIEK LGSLKADLTF DNLKDLPLLE AAIRETLRLH
     PPIFQMMRRV VADKIVYEKN GMEIPKGNFI CAAPGVTQVD PTYFNEPTTY NPYRWIEKTD
     PVHQLEQGDD ANIDYGFGAV GISSKSPFLP FGAGRHRCIG EQFGYLQLKT VISTFIRTFD
     FDLDGKSVPK SDYTSMVVVP EHTAKVRYTW RE
//