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   03-AUG-2022, entry version 114.
DE   RecName: Full=Lanosterol 14-alpha demethylase;
DE            EC=1.14.14.154 {ECO:0000250|UniProtKB:P9WPP9};
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; OrderedLocusNames=Mvan_5161;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
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 vanbaalenii
RT   PYR-1.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   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 C14-
CC       demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol
CC       which is critical for ergosterol biosynthesis. It transforms lanosterol
CC       into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol.
CC       {ECO:0000250|UniProtKB:P9WPP9}.
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:0000250|UniProtKB:P9WPP9};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 1/6.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY575951; AAT40578.1; -; Genomic_DNA.
DR   EMBL; CP000511; ABM15932.1; -; Genomic_DNA.
DR   RefSeq; WP_011782302.1; NC_008726.1.
DR   AlphaFoldDB; Q5IZM4; -.
DR   SMR; Q5IZM4; -.
DR   STRING; 350058.Mvan_5161; -.
DR   PRIDE; Q5IZM4; -.
DR   EnsemblBacteria; ABM15932; ABM15932; Mvan_5161.
DR   KEGG; mva:Mvan_5161; -.
DR   eggNOG; COG2124; Bacteria.
DR   HOGENOM; CLU_001570_15_0_11; -.
DR   OMA; AWTLIEL; -.
DR   OrthoDB; 520970at2; -.
DR   UniPathway; UPA00770; UER00754.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Cytoplasm; Heme; Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT   CHAIN           1..452
FT                   /note="Lanosterol 14-alpha demethylase"
FT                   /id="PRO_0000052018"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         395
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"
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