ID   CP51_CANGA              Reviewed;         533 AA.
AC   P50859; Q02312;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 63.
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=ERG11; Synonyms=CYP51; OrderedLocusNames=CAGL0E04334g;
OS   Candida glabrata (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   mitosporic Nakaseomyces.
OX   NCBI_TaxID=5478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2001-L5;
RX   MEDLINE=96161286; PubMed=8593007;
RA   Geber A., Hitchcock C.A., Swartz J.E., Pullen F.S., Marsden K.E.,
RA   Kwon-Chung K.J., Bennett J.E.;
RT   "Deletion of the Candida glabrata ERG3 and ERG11 genes: effect on cell
RT   viability, cell growth, sterol composition, and antifungal
RT   susceptibility.";
RL   Antimicrob. Agents Chemother. 39:2708-2717(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-473.
RC   STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
RX   MEDLINE=95081364; PubMed=7989540;
RA   Burgener-Kairuz P., Zuber J.P., Jaunin P., Buchman T.G., Bille J.,
RA   Rossier M.;
RT   "Rapid detection and identification of Candida albicans and Torulopsis
RT   (Candida) glabrata in clinical specimens by species-specific nested
RT   PCR amplification of a cytochrome P-450 lanosterol-alpha-demethylase
RT   (L1A1) gene fragment.";
RL   J. Clin. Microbiol. 32:1902-1907(1994).
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; L40389; AAB02329.1; -; Genomic_DNA.
DR   EMBL; CR380951; CAG58795.1; -; Genomic_DNA.
DR   EMBL; S75389; AAB32679.1; -; Genomic_DNA.
DR   RefSeq; XP_445876.1; -.
DR   GeneID; 2887532; -.
DR   KEGG; cgr:CAGL0E04334g; -.
DR   HOGENOM; P50859; -.
DR   OMA; P50859; NFVFPNL.
DR   BRENDA; 1.14.13.70; 189220.
DR   DrugBank; DB00639; Butoconazole.
DR   DrugBank; DB01167; Itraconazole.
DR   DrugBank; DB01110; Miconazole.
DR   GO; GO:0016020; C:membrane; 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   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    533       Lanosterol 14-alpha demethylase.
FT                                /FTId=PRO_0000052004.
FT   METAL       472    472       Iron (heme axial ligand) (By similarity).
FT   CONFLICT     64     64       I -> M (in Ref. 3; AAB32679).
FT   CONFLICT    473    473       I -> T (in Ref. 3; AAB32679).
SQ   SEQUENCE   533 AA;  61305 MW;  A0506C17507E6EF7 CRC64;
     MSTENTSLVV ELLEYVKLGL SYFQALPLAQ RVSIMVALPF VYTITWQLLY SLRKDRPPLV
     FYWIPWVGSA IPYGTKPYEF FEDCQKKYGD IFSFMLLGRI MTVYLGPKGH EFIFNAKLAD
     VSAEAAYSHL TTPVFGKGVI YDCPNHRLME QKKFVKGALT KEAFVRYVPL IAEEIYKYFR
     NSKNFKINEN NSGIVDVMVS QPEMTIFTAS RSLLGKEMRD KLDTDFAYLY SDLDKGFTPI
     NFVFPNLPLE HYRKRDHAQQ AISGTYMSLI KERREKNDIQ NRDLIDELMK NSTYKDGTKM
     TDQEIANLLI GVLMGGQHTS AATSAWCLLH LAERPDVQEE LYQEQMRVLN NDTKELTYDD
     LQNMPLLNQM IKETLRLHHP LHSLFRKVMR DVAIPNTSYV VPRDYHVLVS PGYTHLQEEF
     FPKPNEFNIH RWDGDAASSS AAGGDEVDYG FGAISKGVSS PYLPFGGGRH RCIGELFAYC
     QLGVLMSIFI RTMKWRYPTE GETVPPSDFT SMVTLPTAPA KIYWEKRHPE QKY
//