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 16-JUN-2009, entry version 34. DE RecName: Full=Probable lanosterol 14-alpha demethylase; DE Short=LDM; DE EC=1.14.13.70; DE AltName: Full=Cytochrome P450 51; DE AltName: Full=Sterol 14-demethylase; DE AltName: Full=P450-14DM; GN Name=cyp51; ORFNames=DDB_G0279403; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; 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., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA 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., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA 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 CC critical for ergosterol biosynthesis. It transforms lanosterol CC into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By CC 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 -!- SUBCELLULAR LOCATION: Membrane (Potential). Membrane; Single-pass CC membrane protein. 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; AAFI02000030; EAS66884.1; -; Genomic_DNA. DR RefSeq; XP_001134568.1; -. DR GeneID; 4238117; -. DR KEGG; ddi:DDB_0232962; -. DR dictyBase; DDB_G0279403; cyp51. DR BRENDA; 1.14.13.70; 424. DR GO; GO:0016020; C:membrane; 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; Heme; Iron; Lipid synthesis; Membrane; KW Metal-binding; Monooxygenase; NADP; Oxidoreductase; KW Steroid biosynthesis; Sterol biosynthesis. FT CHAIN 1 466 Probable lanosterol 14-alpha demethylase. FT /FTId=PRO_0000318989. FT METAL 413 413 Iron (heme axial ligand) (By similarity). 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 //