ID   CP51_PENIT              Reviewed;         515 AA.
AC   Q12664;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Eburicol 14-alpha-demethylase;
DE            EC=1.14.14.154;
DE   AltName: Full=CYPLI;
DE   AltName: Full=Cytochrome P450 51;
DE   AltName: Full=Cytochrome P450-14DM;
DE   AltName: Full=Cytochrome P450-LIA1;
DE   AltName: Full=Sterol 14-alpha demethylase;
GN   Name=CYP51;
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W5;
RX   PubMed=8628233; DOI=10.1007/bf02172984;
RA   van Nistelrooy J.G.M., van den Brink J.M., van Kan J.A.L.,
RA   van Gorcom R.F.M., de Waard M.A.;
RT   "Isolation and molecular characterisation of the gene encoding eburicol 14
RT   alpha-demethylase (cYP51) from Penicillium italicum.";
RL   Mol. Gen. Genet. 250:725-733(1996).
CC   -!- FUNCTION: Catalyzes C14-demethylation of lanosterol which is critical
CC       for ergosterol biosynthesis. It transforms lanosterol into 4,4'-
CC       dimethyl cholesta-8,14,24-triene-3-beta-ol.
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}.
CC       Microsome membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Z49750; CAA89824.1; -; Genomic_DNA.
DR   PIR; S65578; S65578.
DR   AlphaFoldDB; Q12664; -.
DR   SMR; Q12664; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB-EC.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..515
FT                   /note="Eburicol 14-alpha-demethylase"
FT                   /id="PRO_0000052008"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         459
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"
SQ   SEQUENCE   515 AA;  58137 MW;  13679B56F8769255 CRC64;
     MDLVPLVTGQ ILGIAYYTTG LFLVSIVLNV IKQLIFYNRK EPPVVFHWIP FIGSTIAYGM
     DPYQFFFASR AKYGDIFTFI LLGKKTTVYL GVEGNEFILN GKLKDVNAEE VYGKLTTPVF
     GSDVVYDCPN SKLMEQKKFI KYGLSQEALE SYVPLIADET NAYIKSSPNF KGQSGTIDLA
     AAMAEITIFT AARTLQGEEV RSKLTSEFAD LFHDLDLGFS PINFMLPWAP LPHNASAIKH
     TTYARDLSGN YPSATGSWRR RQRRRQDKSK GTDMISNLMR CVYRDGTPIP DKEIAHMMIT
     LLMAGQHSSS AISCWILLRL ASQPEMAEKL HAEQIKNLGA DLPPLQYKDM DKLPLLRNVI
     KETLRLHSSI HTLMRKVKNP MPVPGTDFVV PPSHTLLSSP GVTARDERHF RDPLRWDPHR
     WESRVEVEDS SDTVDYGYGA VSKGTRSPYL PFGAGRHRCI GEKFAYLNLE VIVATLVREF
     RFFNPEGMEG VPDTDYSSLF SRPVQPATVR WEVRS