CP51_CANTR
ID CP51_CANTR Reviewed; 528 AA.
AC P14263;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=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 Name=ERG11; Synonyms=CYP51;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX PubMed=3068024; DOI=10.1089/dna.1988.7.617;
RA Chen C., Kalb V.F., Turi T.G., Loper J.C.;
RT "Primary structure of the cytochrome P450 lanosterol 14 alpha-demethylase
RT gene from Candida tropicalis.";
RL DNA 7:617-626(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 434-528.
RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541 / NBRC 1400;
RX PubMed=3304292; DOI=10.1016/0006-291x(87)90792-3;
RA Chen C., Turi T.G., Sanglard D., Loper J.C.;
RT "Isolation of the Candida tropicalis gene for P450 lanosterol demethylase
RT and its expression in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 146:1311-1317(1987).
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 -!- 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}.
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DR EMBL; M23673; AAA53284.1; -; Genomic_DNA.
DR EMBL; M17595; AAA34316.1; -; Genomic_DNA.
DR PIR; A31854; A31854.
DR AlphaFoldDB; P14263; -.
DR SMR; P14263; -.
DR VEuPathDB; FungiDB:CTMYA2_056970; -.
DR VEuPathDB; FungiDB:CTRG_05283; -.
DR UniPathway; UPA00770; UER00754.
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: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 Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..528
FT /note="Lanosterol 14-alpha demethylase"
FT /id="PRO_0000052005"
FT BINDING 470
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 CONFLICT 448
FT /note="G -> V (in Ref. 2; AAA34316)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="V -> G (in Ref. 2; AAA34316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60928 MW; 83F8E3C1C1E826B9 CRC64;
MAIVDTAIDG INYFLSLSLT QQITILVVFP FIYNIAWQLL YSLRKDRVPM VFYWIPWFGS
AASYGMQPYE FFEKCRLKYG DVFSFMLLGK VMTVYLGPKG HEFIYNAKLS DVSAEEAYTH
LTTPVFGKGV IYDCPNSRLM EQKKFAKFAL TTDSFKTYVP KIREEVLNYF VNDVSFKTKE
RDHGVASVMK TQPEITIFTA SRCLFGDEMR KSFDRSFAQL YADLDKGFTP INFVFPNLPL
PHYWRRDAAQ RKISAHYMKE IKRRRESGDI DPKRDLIDSL LVNSTYKDGV KMTDQEIANL
LIGVLMGGQH TSASTSAWFL LHLAEQPQLQ DDLYEELTNL LKEKGGDLND LTYEDLQKLP
LVNNTIKETL RMHMPLHSIF RKVMNPLRVP NTKYVIPKGH YVLVSAGYAH TSDRWFEHPE
HFNPRRWESD DTKASAVSFN SEDTVDYGFG KISKGVSSPY LPFGGGRHRC IGEQFAYVQL
GTILTTYIYN FKWRLNGDKV PDVDYQSMVT LPLEPAEIVW EKRDTCMV
