CP51_CUNEL
ID CP51_CUNEL Reviewed; 512 AA.
AC Q9UVC3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=CYP51;
OS Cunninghamella elegans.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Cunninghamella.
OX NCBI_TaxID=4853;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 36112 / DSM 8217 / PA-1;
RA Craft D.L., Loper J.C.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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; AF046863; AAF20263.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UVC3; -.
DR SMR; Q9UVC3; -.
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..512
FT /note="Lanosterol 14-alpha demethylase"
FT /id="PRO_0000052006"
FT BINDING 458
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 512 AA; 57677 MW; 5E10C9D415CA15B1 CRC64;
MAIVSQISRF ITFTIISMGY SVLAVGVALT IHILSQLIVP KNPNEPPNVF SLIPVLGNAV
QFGMNPVAFL QECQKKYGDV FTFTMVGKRV TVCLGADGNQ FVFNSKQNLS SAAEAYNHMT
KYVFGPDVVY DAPHAVFMEQ KKFIKAGLNS DCFRQHVPMI VQETEEFFKK FNKPTGFIEA
YETFGSLIIY TASRCLMGKE IRASLDGNVA KLYYDLDQGF KPINFIFPNL PLPSYRRRDV
ACKKMADLYS SIIQRRKDEK DNNNADLLQA LMDATYKDGT HIPDHHIAGM MIAVLFGGQH
TSATTSAWTI LELANRPDII KALREEQIEK LGSLKADLTF DNLKDLPLLE AAIRETLRLH
PPIFQMMRRV VADKIVYEKN GMEIPKGNFI CAAPGVTQVD PTYFNEPTTY NPYRWIEKTD
PVHQLEQGDD ANIDYGFGAV GISSKSPFLP FGAGRHRCIG EQFGYLQLKT VISTFIRTFD
FDLDGKSVPK SDYTSMVVVP EHTAKVRYTW RE
