ID   CP51_MYCVP              Reviewed;         452 AA.
AC   Q5IZM4; A1TFI2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Lanosterol 14-alpha demethylase;
DE            EC=1.14.13.70;
DE   AltName: Full=Cytochrome P450 51;
DE   AltName: Full=CYPLI;
DE   AltName: Full=P450-LIA1;
DE   AltName: Full=Sterol 14-alpha demethylase;
DE   AltName: Full=P450-14DM;
GN   Name=cyp51; OrderedLocusNames=Mvan_5161;
OS   Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brezna B., Stingley R.L., Freeman J.P., Khan A.A., Cerniglia C.E.;
RT   "The cytochromes p450 from PAH-degrading strain Mycobacterium
RT   vanbaalenii PYR-1.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Its precise biological substrate is not known. Catalyzes
CC       C14-demethylation of lanosterol, 24,25-dihydrolanosterol and
CC       obtusifoliol which is critical for ergosterol biosynthesis. It
CC       transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-
CC       3-beta-ol (By 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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AY575951; AAT40578.1; -; Genomic_DNA.
DR   EMBL; CP000511; ABM15932.1; -; Genomic_DNA.
DR   RefSeq; YP_955938.1; -.
DR   SMR; Q5IZM4; 7-449.
DR   GeneID; 4647445; -.
DR   GenomeReviews; CP000511_GR; Mvan_5161.
DR   KEGG; mva:Mvan_5161; -.
DR   OMA; Q5IZM4; MEQVTGG.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme 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; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
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; Cytoplasm; Heme; Iron; Lipid synthesis;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW   Steroid biosynthesis; Sterol biosynthesis.
FT   CHAIN         1    452       Lanosterol 14-alpha demethylase.
FT                                /FTId=PRO_0000052018.
FT   METAL       395    395       Iron (heme axial ligand).
SQ   SEQUENCE   452 AA;  51681 MW;  716ED23C210A2ADC CRC64;
     MTAVKEVPRV SGGEEEHGHL EEFRTDPIGL MKRVREECGD VGWFQLADKQ VILLSGAEAN
     EFFFRSSDSE LNQAEAYPFM TPIFGEGVVF DADPERRAEM LHNTALRGEH MKGHATTIEA
     EVRKMIEGWG ESGEIDLLEF FAELTIYTST ACLIGLKFRN QLDSRFANYY HLLERGTDPL
     CYVDPYLPIE SFRIRDEARA GLVELVQDVM HGRIANPPKD KSDRDMLDVL VSIKDEDGNP
     RFTANEITGM FISLMFAGHH TSSGTSSWTL IELLRHPEFY AKVQQELDDL YADGQEVSFH
     ALRQIPSLDN ALKETLRLHP PLIILMRVAQ DEFEVAGYPI HKGQMVAASP AISNRIPEDF
     PNPDDFDPDR YEKPRQEDLI NRWTWIPFGA GKHRCVGAAF AQMQIKAIFS VLLREYEFEM
     AQPPESYQND HSKMVVQLAR PAKVRYRRRV RD
//