ID CP51_MYCBO Reviewed; 451 AA. AC P0A513; P77901; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Lanosterol 14-alpha demethylase; DE EC=1.14.13.70; DE AltName: Full=Cytochrome P450 51; DE AltName: Full=CYPLI; DE AltName: Full=P450-LIA1; DE AltName: Full=Sterol 14-alpha demethylase; DE AltName: Full=P450-14DM; GN Name=cyp51; OrderedLocusNames=Mb0787c; OS Mycobacterium bovis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1765; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., RA Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., RA Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., RA Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). CC -!- FUNCTION: Its precise biological substrate is not known. Catalyzes CC C14-demethylation of lanosterol, 24,25-dihydrolanosterol and CC obtusifoliol which is critical for ergosterol biosynthesis. It CC transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene- CC 3-beta-ol (By similarity). CC -!- CATALYTIC ACTIVITY: Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha- CC methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 CC NADP(+) + 4 H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol CC from lanosterol: step 1/6. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248336; CAD93649.1; -; Genomic_DNA. DR RefSeq; NP_854445.1; -. DR SMR; P0A513; 2-449. DR GeneID; 1092457; -. DR GenomeReviews; BX248333_GR; Mb0787c. DR KEGG; mbo:Mb0787c; -. DR HOGENOM; P0A513; -. DR OMA; P0A513; MEQVTGG. DR BRENDA; 1.14.13.70; 3091. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0008398; F:sterol 14-demethylase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017973; Cyt_P450_C. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002403; Cyt_P450_E_grp-IV. DR Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1. DR PANTHER; PTHR19383; Cyt_P450; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00465; EP450IV. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Heme; Iron; Lipid synthesis; KW Metal-binding; Monooxygenase; NADP; Oxidoreductase; KW Steroid biosynthesis; Sterol biosynthesis. FT CHAIN 1 451 Lanosterol 14-alpha demethylase. FT /FTId=PRO_0000052016. FT METAL 394 394 Iron (heme axial ligand). SQ SEQUENCE 451 AA; 50878 MW; B3D671EA9542A57B CRC64; MSAVALPRVS GGHDEHGHLE EFRTDPIGLM QRVRDECGDV GTFQLAGKQV VLLSGSHANE FFFRAGDDDL DQAKAYPFMT PIFGEGVVFD ASPERRKEML HNAALRGEQM KGHAATIEDQ VRRMIADWGE AGEIDLLDFF AELTIYTSSA CLIGKKFRDQ LDGRFAKLYH ELERGTDPLA YVDPYLPIES FRRRDEARNG LVALVADIMN GRIANPPTDK SDRDMLDVLI AVKAETGTPR FSADEITGMF ISMMFAGHHT SSGTASWTLI ELMRHRDAYA AVIDELDELY GDGRSVSFHA LRQIPQLENV LKETLRLHPP LIILMRVAKG EFEVQGHRIH EGDLVAASPA ISNRIPEDFP DPHDFVPARY EQPRQEDLLN RWTWIPFGAG RHRCVGAAFA IMQIKAIFSV LLREYEFEMA QPPESYRNDH SKMVVQLAQP ACVRYRRRTG V //