ID   CP51_USTMA              Reviewed;         561 AA.
AC   P49602; Q4P8A1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
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=Lanosterol 14-alpha demethylase;
DE   AltName: Full=P450-14DM;
GN   Name=ERG11; Synonyms=CYP51; ORFNames=UM03662;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMI 103761;
RX   MEDLINE=96275901; PubMed=8674989; DOI=10.1016/0378-1097(96)00142-5;
RA   Hargreaves J.A., Keon J.P.R.;
RT   "Isolation of an Ustilago maydis ERG11 gene and its expression in a
RT   mutant deficient in sterol 14 alpha-demethylase activity.";
RL   FEMS Microbiol. Lett. 139:203-207(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
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; Z48164; CAA88176.1; -; Genomic_DNA.
DR   EMBL; AACP01000124; EAK84840.1; -; Genomic_DNA.
DR   PIR; S52319; S52319.
DR   RefSeq; XP_759809.1; -.
DR   HSSP; P77901; 1E9X.
DR   GeneID; 3631809; -.
DR   KEGG; uma:UM03662.1; -.
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    561       Cytochrome P450 51.
FT                                /FTId=PRO_0000052011.
FT   METAL       501    501       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   561 AA;  62197 MW;  2F9A6647D9B17FB0 CRC64;
     MVASSSSATA SLLDQLFALT PLADSSAWIK TITVLVLLPL LAVVLNVASQ LLLATPKNHP
     PVVFHFVPVI GSAIYYGIDP YKFFFECREK YGDVFTFVLL GRKITVALGP KGSNLVFNAK
     HQQVTAEDAY THLTTPVFGK EVVYDVPNAV FMEQKKFVKV GLSIENFRVY VPQIVDEVRE
     YIKSDARFSA LKTRKTITVD IFQAMSELII LTASRTLQGK EVRQGLDKSF AQLYHDLDSG
     FTPINFVIPN LPLPSNFKRD RAQKKMSQFY QDIVAKRRAA GASTSADDAS GENDMIAALI
     EQKYKNGRAL SGVEIAHMMI ALLMAGQHTS SATSSWAFLR LASRPEIIEE LYEEQLNVYS
     DGHGGLRELD YETQKTSVPL LDAVVKETLR LHPPLHSIMR YVKSDLAVPP TLSSPTSTKS
     EPDAHYVIPK GHYIMAAPGV SQVDPQIWKS SDQFDPHRWL DATTAAAMQD SGEDKQDFGF
     GMISTGANSP YLPFGAGRHR CIGEQFAYLQ IGVILATFVR IFKWHLDSKF PDPDYQSMVV
     LPSKNGCAIV LTPRAESLHL D
//