ID   CP51_MIMIV              Reviewed;         709 AA.
AC   Q5UQI3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Probable lanosterol 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   OrderedLocusNames=MIMI_L808;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   FUNCTION.
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=19515774; DOI=10.1128/jvi.00289-09;
RA   Lamb D.C., Lei L., Warrilow A.G., Lepesheva G.I., Mullins J.G.,
RA   Waterman M.R., Kelly S.L.;
RT   "The first virally encoded cytochrome p450.";
RL   J. Virol. 83:8266-8269(2009).
CC   -!- FUNCTION: Catalyzes the 14-alpha demethylation of obtusifoliol to 4
CC       alpha-methyl-5 alpha-ergosta-8,14,24(28)-trien-3 beta-ol. {ECO:0000250,
CC       ECO:0000269|PubMed:19515774}.
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   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY653733; AAV51068.1; -; Genomic_DNA.
DR   RefSeq; YP_003987340.1; NC_014649.1.
DR   SMR; Q5UQI3; -.
DR   PRIDE; Q5UQI3; -.
DR   GeneID; 9925470; -.
DR   KEGG; vg:9925470; -.
DR   UniPathway; UPA00770; UER00754.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0016020; C:membrane; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008398; F:sterol 14-demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   Gene3D; 2.60.120.590; -; 1.
DR   InterPro; IPR037151; AlkB-like_sf.
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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Methyltransferase; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase.
FT   CHAIN           1..709
FT                   /note="Probable lanosterol 14-alpha demethylase"
FT                   /id="PRO_0000052015"
FT   BINDING         425
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   709 AA;  82186 MW;  FCE6AF553DEF2F6F CRC64;
     MLFELSIGAI IGFLTLYLLK RFNESKNFIT PDNLKKIPIV EGAVPVLGHG PAFSKDIMQF
     MKNCYKKYGS VFQLKIFRTN MVVLCDRKLS EEFFKSREND MSLYDVLNRL FFGLAFSDKP
     DSLEFIIKMV KKTITIRYDD FAPKIMDEAQ RLTKIMRESH SGKKLDMIPE IIKFVSRTSA
     RCFIAMDIDD EFYDALNKFT NLLNKIVVLT YFVPHWLLNA TLNRFMLRKY RMRMTKLLEN
     EIEKYRTDLN KSDSLLFRKC VDHIDPETGA TLTNQDIGDI VVCLLYVSSE NTSLLATNCL
     IDLTLNPKYW DLIKSECSAM IALGDYKNLF KAPLLNSIVM ESARLNSHVF ALARKPKTVN
     RIGDYFVADN VDTISLCEPA LMKFEIASDV YANPNSYDPV RFMAPRNEPK DSGHVMNWGK
     GVHECPGKQF AIYEVKAAIA YIVTNFERFE FNHNDLKINY FSPSAMCEKN ISVEFIPSQQ
     NIHNIVYKDR TYIVEHIKCN ETSAWLIYNA LDRQQQREYY QYTYEISTDS QEHKLIEKAG
     PHKPFPIAYD KLVYTGQSNC MTPTKWYDFA SDIWELLTEN YAELGFPIYD DKIRNFVPNS
     FYGQLYSVES IMPTHRDQHV DYGLSISIGS NCEFVIEDKT ILLPSGSVLI GDFSKISHSV
     SKIFHEKPDH LSDFEFFNRV RFSAQIRSID PDVQPLMTTQ EFLDMISEY