ID CP51_PENIT Reviewed; 515 AA. AC Q12664; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 25-NOV-2008, entry version 49. DE RecName: Full=Cytochrome P450 51; DE EC=1.14.13.70; DE AltName: Full=CYPLI; DE AltName: Full=P450-LIA1; DE AltName: Full=Sterol 14-alpha demethylase; DE AltName: Full=Eburicol 14-alpha-demethylase; DE AltName: Full=P450-14DM; GN Name=CYP51; OS Penicillium italicum. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Penicillium. OX NCBI_TaxID=40296; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=W5; RX MEDLINE=96204513; PubMed=8628233; DOI=10.1007/s004380050126; RA van Nistelrooy J.G.M., van den Brink J.M., van Kan J.A.L., RA van Gorcom R.F.M., de Waard M.A.; RT "Isolation and molecular characterisation of the gene encoding RT eburicol 14 alpha-demethylase (cYP51) from Penicillium italicum."; RL Mol. Gen. Genet. 250:725-733(1996). 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane (Potential). CC Microsome membrane (Potential). 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; Z49750; CAA89824.1; -; Genomic_DNA. DR PIR; S65578; S65578. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005792; C:microsome; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 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: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; 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 Endoplasmic reticulum; Heme; Iron; Lipid synthesis; Membrane; KW Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; KW Steroid biosynthesis; Sterol biosynthesis; Transmembrane. FT CHAIN 1 515 Cytochrome P450 51. FT /FTId=PRO_0000052008. FT TRANSMEM 11 31 Potential. FT METAL 459 459 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 515 AA; 58137 MW; 13679B56F8769255 CRC64; MDLVPLVTGQ ILGIAYYTTG LFLVSIVLNV IKQLIFYNRK EPPVVFHWIP FIGSTIAYGM DPYQFFFASR AKYGDIFTFI LLGKKTTVYL GVEGNEFILN GKLKDVNAEE VYGKLTTPVF GSDVVYDCPN SKLMEQKKFI KYGLSQEALE SYVPLIADET NAYIKSSPNF KGQSGTIDLA AAMAEITIFT AARTLQGEEV RSKLTSEFAD LFHDLDLGFS PINFMLPWAP LPHNASAIKH TTYARDLSGN YPSATGSWRR RQRRRQDKSK GTDMISNLMR CVYRDGTPIP DKEIAHMMIT LLMAGQHSSS AISCWILLRL ASQPEMAEKL HAEQIKNLGA DLPPLQYKDM DKLPLLRNVI KETLRLHSSI HTLMRKVKNP MPVPGTDFVV PPSHTLLSSP GVTARDERHF RDPLRWDPHR WESRVEVEDS SDTVDYGYGA VSKGTRSPYL PFGAGRHRCI GEKFAYLNLE VIVATLVREF RFFNPEGMEG VPDTDYSSLF SRPVQPATVR WEVRS //