CP51_ASHGO
ID CP51_ASHGO Reviewed; 529 AA.
AC Q759W0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; OrderedLocusNames=ADR162W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR EMBL; AE016817; AAS52083.1; -; Genomic_DNA.
DR RefSeq; NP_984259.1; NM_209612.1.
DR AlphaFoldDB; Q759W0; -.
DR SMR; Q759W0; -.
DR STRING; 33169.AAS52083; -.
DR EnsemblFungi; AAS52083; AAS52083; AGOS_ADR162W.
DR GeneID; 4620421; -.
DR KEGG; ago:AGOS_ADR162W; -.
DR eggNOG; KOG0684; Eukaryota.
DR HOGENOM; CLU_001570_15_0_1; -.
DR InParanoid; Q759W0; -.
DR OMA; AWTLIEL; -.
DR UniPathway; UPA00770; UER00754.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
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:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008398; F:sterol 14-demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..529
FT /note="Lanosterol 14-alpha demethylase"
FT /id="PRO_0000052002"
FT BINDING 468
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 529 AA; 60506 MW; BE674CB09ABD67DA CRC64;
MSESLLQTVV AYVELVLHHF MALSWTQQLS IVIVAPFIYS LVWQTLYSFR KDRVPLVPFM
VPWVGSALAY GRAPYEFFGK CQQKYGDVFA FMLLGRVMTV YLGTKGHEFI LNAKLAEVSA
EEAYTKLTTP VFGEGVVYDC PNHRLMEQKK FCKNALSTEA FRRYVPMVMD EVRKYLRTSK
HFMMNERSSG VVNVMETQPE MTIFTASRSL LGAEMHSMLD ADFAYLYADL DKGFTPLNFV
FRDLPLDNYR RRDNAQRTIS STYMKVIERR RKNNDVQDRD LIDALMTSAQ YKDGVKMTDQ
QIANLLIGVL MGGQHTSAAT SAWVLLHLAE RPDIQEELYE EQMRVLDGGA KELTYELLQE
MPLLNQVIKE TLRMHHPLHS LFRKVTRDMP VPNTSYVIPK DHYVLASPGF CHLSEEYFPN
AKEFNPHRWD NDAASSVSTG EKVDYGFGAI SKGVSSPYLP FGGGRHRCIG EGFAYMQLGT
IFSVVVRSMK WHFPADMKGV PNPDFTSMVT LPSEPCRIAW ERRVPDQII
