CP51_PICKU
ID CP51_PICKU Reviewed; 414 AA.
AC Q02315;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
DE Flags: Fragment;
GN Name=CYP51;
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6258 / CBS 573 / DSM 6128 / JCM 1609 / NBRC 1064 / NRRL Y-413;
RX PubMed=7989540; DOI=10.1128/jcm.32.8.1902-1907.1994;
RA Burgener-Kairuz P., Zuber J.P., Jaunin P., Buchman T.G., Bille J.,
RA Rossier M.;
RT "Rapid detection and identification of Candida albicans and Torulopsis
RT (Candida) glabrata in clinical specimens by species-specific nested PCR
RT amplification of a cytochrome P-450 lanosterol-alpha-demethylase (L1A1)
RT gene fragment.";
RL J. Clin. Microbiol. 32:1902-1907(1994).
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; S75391; AAB32680.1; -; Genomic_DNA.
DR AlphaFoldDB; Q02315; -.
DR SMR; Q02315; -.
DR VEuPathDB; FungiDB:C5L36_0D02200; -.
DR eggNOG; KOG0684; Eukaryota.
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; 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.
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..>414
FT /note="Lanosterol 14-alpha demethylase"
FT /id="PRO_0000052007"
FT NON_TER 414
SQ SEQUENCE 414 AA; 46981 MW; A23CCD0EE1F3A72D CRC64;
MPWVGSAVVY GMQPYEFFEN CRKQHGDVFS FLLLGKVMTV YLGPKGHEFV LNAKLSDVSA
EDAYTHLTTP VFGKGVIYDC PNWKLMEQKK FAKVALTKES FIRYVPLIKD EMLKYFNANF
RGDSGKTDVL KSQSEMTLFT ASRSLFGDAL RNRLDASYAE MYSDLDKGFT PLNFVFSYLP
LPNYWKRDAA HKNISNTYLD LINTKRAGGE IKNEDLVDAL LKNSVYKDGT RMTDEELAHL
MIGVLMGGQH TSSATSAWFL LHLGEKPQLQ EEIYREIQSV LGENFERELT YDDLQKLDLV
NATIKETLRL HMPLHSIFRK VTRDLPVPNT SYIVPKGHYV LISPGYTMLS ERYFPNASEF
QPHRWDEIKS IDGGISFGAE GENAKETVDY GFGKISKGVA SPYLPFGGGR HRCT
