CP51_DICDI
ID CP51_DICDI Reviewed; 466 AA.
AC Q1ZXH9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable lanosterol 14-alpha demethylase;
DE Short=LDM;
DE EC=1.14.14.154;
DE AltName: Full=Cytochrome P450 51;
DE AltName: Full=Cytochrome P450-14DM;
DE AltName: Full=Sterol 14-demethylase;
GN Name=cyp51; ORFNames=DDB_G0279403;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000030; EAS66884.1; -; Genomic_DNA.
DR RefSeq; XP_001134568.1; XM_001134568.1.
DR AlphaFoldDB; Q1ZXH9; -.
DR SMR; Q1ZXH9; -.
DR STRING; 44689.DDB0232962; -.
DR PaxDb; Q1ZXH9; -.
DR EnsemblProtists; EAS66884; EAS66884; DDB_G0279403.
DR GeneID; 8622003; -.
DR KEGG; ddi:DDB_G0279403; -.
DR dictyBase; DDB_G0279403; cyp51.
DR eggNOG; KOG0684; Eukaryota.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q1ZXH9; -.
DR OMA; AWTLIEL; -.
DR PhylomeDB; Q1ZXH9; -.
DR Reactome; R-DDI-191273; Cholesterol biosynthesis.
DR Reactome; R-DDI-211976; Endogenous sterols.
DR UniPathway; UPA00770; UER00754.
DR PRO; PR:Q1ZXH9; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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..466
FT /note="Probable lanosterol 14-alpha demethylase"
FT /id="PRO_0000318989"
FT BINDING 413
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 466 AA; 52686 MW; 96E98F64C579EA90 CRC64;
MIGTIAVLVI AILVIFAFKK SPSNIPPIVE TIPFIGCFYQ FAKNPLQLVR NSYDRLGEIF
TLHLMGFKMT FVLGPEAQAL FFRGTDEELS PKEAYRFVTP VFGKGVVYDS ETEIMYEQLR
FVKNGLVLSQ LKKAVGIIQE ETEKYFETKW GDSGEIDLLY EMNKLTILTA SRCLMGKSIN
KSLGQSGQLA DLYHELEEGL NPISFFFPNL PLPSFKKRDA ARAKVAAIFH SIIQERRRST
DDSVDDVLYT LMNSKYKDGS VLEDEQIVGL MIGLLFAGQH TSSITLTYTI FYLLNNLEYF
DETQKDINDI VQKENQGEIN FDGLKRMNRL ETVIREVLRL HPPLIFLMRK VMTPMEYKGK
TIPAGHILAV SPQVGMRLPT VYKNPDSFEP KRFDVEDKTP FSFIAFGGGK HGCPGENFGI
LQIKTIWTVL STKYNLEVGP VPPTDFTSLV AGPKGPCMVK YSKKQK
