ID ERG7_SCHPO Reviewed; 721 AA. AC Q10231; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 05-MAY-2009, entry version 64. DE RecName: Full=Lanosterol synthase; DE EC=5.4.99.7; DE AltName: Full=Oxidosqualene--lanosterol cyclase; DE Short=OSC; DE AltName: Full=2,3-epoxysqualene--lanosterol cyclase; GN Name=erg7; ORFNames=SPAC13G7.01c, SPAC4G9.21c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96193650; PubMed=8604986; DOI=10.1006/bbrc.1996.0232; RA Corey E.J., Matsuda S.P.T., Baker C.H., Ting A.Y., Cheng H.; RT "Molecular cloning of a Schizosaccharomyces pombe cDNA encoding RT lanosterol synthase and investigation of conserved tryptophan RT residues."; RL Biochem. Biophys. Res. Commun. 219:327-331(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Catalyzes the cyclization of (S)-2,3 oxidosqualene to CC lanosterol, a reaction that forms the sterol nucleus. CC -!- CATALYTIC ACTIVITY: (S)-2,3-epoxysqualene = lanosterol. CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol CC from farnesyl-PP: step 3/3. CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family. CC -!- SIMILARITY: Contains 4 PFTB repeats. 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; U41368; AAA92502.1; -; mRNA. DR EMBL; CU329670; CAA93571.1; -; Genomic_DNA. DR PIR; JC4643; JC4643. DR RefSeq; NP_593702.2; -. DR GeneID; 2542882; -. DR KEGG; spo:SPAC13G7.01c; -. DR GeneDB_Spombe; SPAC13G7.01c; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-002010-MON; -. DR BRENDA; 5.4.99.7; 653. DR ArrayExpress; Q10231; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0000250; F:lanosterol synthase activity; IEA:EC. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001330; Prenyltrans. DR InterPro; IPR018333; Squalene_cyclase. DR InterPro; IPR002365; Terpene_synthase_CS. DR Pfam; PF00432; Prenyltrans; 3. DR TIGRFAMs; TIGR01787; squalene_cyclas; 1. DR PROSITE; PS01074; TERPENE_SYNTHASES; 1. PE 2: Evidence at transcript level; KW Complete proteome; Isomerase; Lipid synthesis; Repeat; KW Steroid biosynthesis. FT CHAIN 1 721 Lanosterol synthase. FT /FTId=PRO_0000072656. FT REPEAT 121 162 PFTB 1. FT REPEAT 555 595 PFTB 2. FT REPEAT 604 645 PFTB 3. FT REPEAT 662 703 PFTB 4. FT ACT_SITE 229 229 Proton acceptor (By similarity). FT ACT_SITE 451 451 Proton donor (By similarity). SQ SEQUENCE 721 AA; 82819 MW; 445B67F4BF7BFBA3 CRC64; MEACRVRPEL SKTVEQIDKS LWRLNIDSAG GETWEYVTKE EAEKRPLTIA EKYFLGFDLD LPKRPPAKTP LESAEYGYEF FRRLQLPDGH WASPYEGPMF LICGAVFAFY ISQTPFPKGW APEIIQYLIN HTNDDGGWGI HTEGVSTVFG TSMNYVVLRI LGMDAGHPVA TRARNRLHEL GGAIGCPHWG KFWLATLNCY DWDGVNPIPP ELWLLPDWIP FHPGKWWCHV RLVYLPMGYM YGERLKCPKD SLIMQLRKEL YVENYDSINF ADHRNTISDV DLYFPHTQIL DRLNWILEKY FTYLRPSWLK KLGTRRAYEL IKIEDQNTDY SCIGPVNAAM NTVCVYFHEG PSSKAFQKHI QRLHDFMWVQ PEGMLMRGTN GLQVWETSFT LQALVESGLY EKEAFKPDIA KALEFLDRQQ IRTQYEGSGY RYNSLGAWPF SNITQGYTVS DTTSEALRAV LLVQSLPDFE KLVDIPRLRL SVDVILGMQN ENLGFASYEP ARTGEWMELL NPAEVFGNIM VEYSYPECTT SVILALRAFT KYDPGYRRDE IENTIENALE YVVKMQRPDG SWYGSWAICF TYAAMFATGS LASAGRYYEN CPVQKKACEF LLSKQRPDGG WSESYMACVT GVYTETESSL VTQTGWALDA LINAKYPDRK PIEKGIKFLM ASQKSDGSWQ QKSMEGIFNK NVAIAYPNYK LYFSIYTLGK FAKQYGNYLT I //