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Database: UniProt
Entry: Q09736
LinkDB: Q09736
Original site: Q09736 
ID   CP51_SCHPO              Reviewed;         495 AA.
AC   Q09736;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Lanosterol 14-alpha demethylase erg11 {ECO:0000303|PubMed:16537923};
DE            EC=1.14.14.154 {ECO:0000305|PubMed:27585850};
DE   AltName: Full=Cytochrome P450 51 {ECO:0000305};
DE   AltName: Full=Ergosterol biosynthetic protein 11 {ECO:0000303|PubMed:16537923};
DE   AltName: Full=Sterol 14-alpha demethylase {ECO:0000305};
GN   Name=erg11 {ECO:0000303|PubMed:16537923}; Synonyms=cyp51;
GN   ORFNames=SPAC13A11.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=8586261; DOI=10.1111/j.1574-6968.1995.tb07929.x;
RA   Harmouch N., Coulon J., Bonaly R.;
RT   "Identification of 24-methylene-24,25-dihydrolanosterol as a precursor of
RT   ergosterol in the yeasts Schizosaccharomyces pombe and Schizosaccharomyces
RT   octosporus.";
RL   FEMS Microbiol. Lett. 134:147-152(1995).
RN   [3]
RP   IDENTIFICATION, AND INDUCTION.
RX   PubMed=16537923; DOI=10.1128/mcb.26.7.2817-2831.2006;
RA   Todd B.L., Stewart E.V., Burg J.S., Hughes A.L., Espenshade P.J.;
RT   "Sterol regulatory element binding protein is a principal regulator of
RT   anaerobic gene expression in fission yeast.";
RL   Mol. Cell. Biol. 26:2817-2831(2006).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DAP1.
RX   PubMed=17276356; DOI=10.1016/j.cmet.2006.12.009;
RA   Hughes A.L., Powell D.W., Bard M., Eckstein J., Barbuch R., Link A.J.,
RA   Espenshade P.J.;
RT   "Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes.";
RL   Cell Metab. 5:143-149(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=18310029; DOI=10.1099/mic.0.2007/011155-0;
RA   Iwaki T., Iefuji H., Hiraga Y., Hosomi A., Morita T., Giga-Hama Y.,
RA   Takegawa K.;
RT   "Multiple functions of ergosterol in the fission yeast Schizosaccharomyces
RT   pombe.";
RL   Microbiology 154:830-841(2008).
RN   [7]
RP   FUNCTION, MUTAGENESIS OF GLY-189, AND PATHWAY.
RX   PubMed=27585850; DOI=10.1534/genetics.116.191536;
RA   Xu Y.J., Singh A., Alter G.M.;
RT   "Hydroxyurea induces cytokinesis arrest in cells expressing a mutated
RT   sterol-14alpha-demethylase in the egosterol biosynthesis pathway.";
RL   Genetics 204:959-973(2016).
RN   [8]
RP   FUNCTION.
RX   PubMed=28893786; DOI=10.1128/aac.00734-17;
RA   Singh A., Agarwal A., Xu Y.J.;
RT   "Novel cell-killing mechanisms of hydroxyurea and the implication toward
RT   combination therapy for the treatment of fungal infections.";
RL   Antimicrob. Agents Chemother. 61:0-0(2017).
CC   -!- FUNCTION: Sterol 14alpha-demethylase that plays a critical role in the
CC       third module of ergosterol biosynthesis pathway, being ergosterol the
CC       major sterol component in fungal membranes that participates in a
CC       variety of functions (PubMed:27585850, PubMed:28893786) (Probable). The
CC       third module or late pathway involves the ergosterol synthesis itself
CC       through consecutive reactions that mainly occur in the endoplasmic
CC       reticulum (ER) membrane (By similarity). In filamentous fungi, during
CC       the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-
CC       ol) can be metabolized to eburicol (By similarity). Sterol 14alpha-
CC       demethylase catalyzes the three-step oxidative removal of the 14alpha-
CC       methyl group (C-32) of both these sterols in the form of formate, and
CC       converts eburicol and lanosterol to 14-demethyleburicol (4,4,24-
CC       trimethylergosta-8,14,24(28)-trienol) and 4,4-dimethyl-5alpha-cholesta-
CC       8,14,24-trien-3beta-ol, respectively, which are further metabolized by
CC       other enzymes in the pathway to ergosterol (Probable). Can also use
CC       substrates not intrinsic to fungi, such as 24,25-dihydrolanosterol
CC       (DHL), producing 4,4-dimethyl-8,14-cholestadien-3-beta-ol, but at lower
CC       rates than the endogenous substrates (By similarity).
CC       {ECO:0000250|UniProtKB:P10614, ECO:0000250|UniProtKB:Q4WNT5,
CC       ECO:0000269|PubMed:27585850, ECO:0000269|PubMed:28893786,
CC       ECO:0000305|PubMed:18310029, ECO:0000305|PubMed:8586261}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--
CC         hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4
CC         H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:138029, ChEBI:CHEBI:138031; EC=1.14.14.154;
CC         Evidence={ECO:0000305|PubMed:27585850};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54029;
CC         Evidence={ECO:0000305|PubMed:27585850};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-methyl steroid + O2 + reduced [NADPH--hemoprotein
CC         reductase] = a 14alpha-hydroxymethyl steroid + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68060, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:138029, ChEBI:CHEBI:176901;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68061;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-hydroxymethyl steroid + O2 + reduced [NADPH--
CC         hemoprotein reductase] = a 14alpha-formyl steroid + H(+) + 2 H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68064,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:176901, ChEBI:CHEBI:176902;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68065;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 14alpha-formyl steroid + O2 + reduced [NADPH--hemoprotein
CC         reductase] = a Delta(14) steroid + formate + 2 H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:68068, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138031,
CC         ChEBI:CHEBI:176902; Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68069;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lanosterol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 4
CC         H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:25286, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16521, ChEBI:CHEBI:17813,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.154;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25287;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lanosterol + O2 + reduced [NADPH--hemoprotein reductase] = 32-
CC         hydroxylanosterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:75103, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16521, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:166806; Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75104;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=32-hydroxylanosterol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 32-oxolanosterol + H(+) + 2 H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:75107, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:166681, ChEBI:CHEBI:166806;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75108;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=32-oxolanosterol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 2
CC         H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:75111, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:17813, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:166681;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75112;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eburicol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC         14-demethyleburicol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:75439, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:70315, ChEBI:CHEBI:194330;
CC         Evidence={ECO:0000250|UniProtKB:P10613};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75440;
CC         Evidence={ECO:0000250|UniProtKB:P10613};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eburicol + O2 + reduced [NADPH--hemoprotein reductase] = 32-
CC         hydroxyeburicol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:75427, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:70315,
CC         ChEBI:CHEBI:194328; Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75428;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=32-hydroxyeburicol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 32-oxoeburicol + H(+) + 2 H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:75431, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:194328, ChEBI:CHEBI:194329;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75432;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=32-oxoeburicol + O2 + reduced [NADPH--hemoprotein reductase] =
CC         14-demethyleburicol + formate + 2 H(+) + H2O + oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:75435, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:194329, ChEBI:CHEBI:194330;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75436;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P10614};
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 1/6. {ECO:0000269|PubMed:27585850}.
CC   -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC       {ECO:0000269|PubMed:27585850}.
CC   -!- SUBUNIT: Interacts with dap1. {ECO:0000269|PubMed:17276356}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is anaerobically up-regulated via the sterol
CC       regulatory element binding protein sre1. {ECO:0000269|PubMed:16537923}.
CC   -!- MISCELLANEOUS: In Aspergillus, the biosynthesis pathway of the sterol
CC       precursors leading to the prevalent sterol ergosterol differs from
CC       yeast. The ringsystem of lanosterol in S.cerevisiae is firstly
CC       demethylised in three enzymatic steps leading to the intermediate
CC       zymosterol and secondly a methyl group is added to zymosterol by the
CC       sterol 24-C-methyltransferase to form fecosterol. In Aspergillus,
CC       lanosterol is firstly transmethylated by the sterol 24-C-
CC       methyltransferase leading to the intermediate eburicol and secondly
CC       demethylated in three steps to form fecosterol. In the genus
CC       Schizosaccharomyces, 2 routes exist from lanosterol to erposterol: the
CC       classical one via zymosterol and the second one via the formation of
CC       eburicol followed by demethylation. {ECO:0000269|PubMed:8586261}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA90803.1; -; Genomic_DNA.
DR   PIR; T37609; T37609.
DR   RefSeq; NP_592990.1; NM_001018389.2.
DR   AlphaFoldDB; Q09736; -.
DR   SMR; Q09736; -.
DR   BioGRID; 279053; 8.
DR   STRING; 284812.Q09736; -.
DR   iPTMnet; Q09736; -.
DR   MaxQB; Q09736; -.
DR   PaxDb; 4896-SPAC13A11-02c-1; -.
DR   EnsemblFungi; SPAC13A11.02c.1; SPAC13A11.02c.1:pep; SPAC13A11.02c.
DR   GeneID; 2542599; -.
DR   KEGG; spo:SPAC13A11.02c; -.
DR   PomBase; SPAC13A11.02c; erg11.
DR   VEuPathDB; FungiDB:SPAC13A11.02c; -.
DR   eggNOG; KOG0684; Eukaryota.
DR   HOGENOM; CLU_001570_15_0_1; -.
DR   InParanoid; Q09736; -.
DR   OMA; AWTLIEL; -.
DR   PhylomeDB; Q09736; -.
DR   Reactome; R-SPO-191273; Cholesterol biosynthesis.
DR   Reactome; R-SPO-211976; Endogenous sterols.
DR   UniPathway; UPA00768; -.
DR   UniPathway; UPA00770; UER00754.
DR   PRO; PR:Q09736; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:PomBase.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; ISS:PomBase.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR   CDD; cd11042; CYP51-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR   PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="Lanosterol 14-alpha demethylase erg11"
FT                   /id="PRO_0000052009"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         442
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         189
FT                   /note="G->D: In erg11-1: Impairs the production of
FT                   ergosterol and leads to hydroxyurea hypersensitivity."
FT                   /evidence="ECO:0000269|PubMed:27585850"
SQ   SEQUENCE   495 AA;  56331 MW;  193333395F6C8B31 CRC64;
     MAFSLVSILL SIALAWYVGY IINQLTSRNS KRPPIVFHWI PFVGSAVAYG MDPYVFFREC
     RAKYGDVFTF VCMGRKMTAF LGVQGNDFLF NGKLADLNAE EAYSHLTTPV FGKDVVYDIP
     NHVFMEHKKF IKSGLGFSQF RSYVPLILNE MDAFLSTSPD FGPGKEGVAD LLKTMPVMTI
     YTASRTLQGA EVRKGFDAGF ADLYHDLDQG FSPVNFVFPW LPLPRNRRRD RAHKIMQKTY
     LKIIKDRRSS TENPGTDMIW TLMSCKYRDG RPLKEHEIAG MMIALLMAGQ HTSAATIVWV
     LALLGSKPEI IEMLWEEQKR VVGENLELKF DQYKDMPLLN YVIQETLRLH PPIHSHMRKV
     KRDLPVPGSK IVIPANNYLL AAPGLTATEE EYFTHATDFD PKRWNDRVNE DENAEQIDYG
     YGLVTKGAAS PYLPFGAGRH RCIGEQFAYM HLSTIISKFV HDYTWTLIGK VPNVDYSSMV
     ALPLGPVKIA WKRRN
//
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