ID FPPS_YEAST Reviewed; 352 AA. AC P08524; D6VW20; P15495; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 2. DT 14-DEC-2011, entry version 113. DE RecName: Full=Farnesyl pyrophosphate synthase; DE Short=FPP synthase; DE Short=FPS; DE EC=2.5.1.10; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1; DE AltName: Full=Farnesyl diphosphate synthase; DE AltName: Full=Geranyltranstransferase; GN Name=ERG20; Synonyms=BOT3, FDS1, FPP1; OrderedLocusNames=YJL167W; GN ORFNames=J0525; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90037051; PubMed=2681213; RA Anderson M.S., Yarger J.G., Burck C.L., Poulter C.D.; RT "Farnesyl diphosphate synthetase. Molecular cloning, sequence, and RT expression of an essential gene from Saccharomyces cerevisiae."; RL J. Biol. Chem. 264:19176-19184(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=96208490; PubMed=8641269; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., RA Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., RA Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., RA Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., RA Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., RA Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., RA Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., RA Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., RA Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., RA Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., RA Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT X."; RL EMBO J. 15:2031-2049(1996). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-352. RX MEDLINE=87246620; PubMed=3036507; RX DOI=10.1111/j.1432-1033.1987.tb11455.x; RA Maarse A.C., Grivell L.A.; RT "Nucleotide sequence of the gene encoding the 11-kDa subunit of the RT ubiquinol-cytochrome-c oxidoreductase in Saccharomyces cerevisiae."; RL Eur. J. Biochem. 165:419-425(1987). RN [5] RP MUTANT GLU-197. RC STRAIN=LB25; RX MEDLINE=93216120; PubMed=8096487; DOI=10.1016/0378-1119(93)90326-X; RA Blanchard L., Karst F.; RT "Characterization of a lysine-to-glutamic acid mutation in a RT conservative sequence of farnesyl diphosphate synthase from RT Saccharomyces cerevisiae."; RL Gene 125:185-189(1993). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC pyrophosphate with the allylic pyrophosphates, dimethylallyl CC pyrophosphate, and then with the resultant geranylpyrophosphate to CC the ultimate product farnesyl pyrophosphate. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl CC diphosphate = diphosphate + geranyl diphosphate. CC -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate CC = diphosphate + (2E,6E)-farnesyl diphosphate. CC -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity). CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate CC biosynthesis; farnesyl diphosphate from geranyl diphosphate and CC isopentenyl diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate CC biosynthesis; geranyl diphosphate from dimethylallyl diphosphate CC and isopentenyl diphosphate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase 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; J05091; AAA34606.1; -; Genomic_DNA. DR EMBL; Z49442; CAA89462.1; -; Genomic_DNA. DR EMBL; X05550; CAA29064.1; -; Genomic_DNA. DR EMBL; BK006943; DAA08636.1; -; Genomic_DNA. DR PIR; A34441; A34441. DR RefSeq; NP_012368.1; NM_001181600.1. DR ProteinModelPortal; P08524; -. DR DIP; DIP-1163N; -. DR IntAct; P08524; 8. DR MINT; MINT-555012; -. DR STRING; P08524; -. DR PeptideAtlas; P08524; -. DR EnsemblFungi; YJL167W; YJL167W; YJL167W. DR GeneID; 853272; -. DR KEGG; sce:YJL167W; -. DR NMPDR; fig|4932.3.peg.3332; -. DR CYGD; YJL167w; -. DR SGD; S000003703; ERG20. DR eggNOG; fuNOG05213; -. DR GeneTree; EFGT00050000002300; -. DR HOGENOM; HBG328346; -. DR OMA; RDFMAVF; -. DR OrthoDB; EOG4SFDFW; -. DR BioCyc; MetaCyc:MONOMER-655; -. DR NextBio; 973547; -. DR ArrayExpress; P08524; -. DR Genevestigator; P08524; -. DR GermOnline; YJL167W; Saccharomyces cerevisiae. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:SGD. DR GO; GO:0004337; F:geranyltranstransferase activity; IDA:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IDA:SGD. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR008949; Terpenoid_synth. DR Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1. DR KO; K00787; -. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; Terpenoid_synth; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW Cholesterol biosynthesis; Complete proteome; Cytoplasm; KW Isoprene biosynthesis; Lipid synthesis; Magnesium; Metal-binding; KW Reference proteome; Steroid biosynthesis; Sterol biosynthesis; KW Transferase. FT CHAIN 1 352 Farnesyl pyrophosphate synthase. FT /FTId=PRO_0000123952. FT METAL 100 100 Magnesium 1 (By similarity). FT METAL 100 100 Magnesium 2 (By similarity). FT METAL 104 104 Magnesium 1 (By similarity). FT METAL 104 104 Magnesium 2 (By similarity). FT METAL 240 240 Magnesium 3 (By similarity). FT BINDING 52 52 Isopentenyl diphosphate (By similarity). FT BINDING 55 55 Isopentenyl diphosphate (By similarity). FT BINDING 93 93 Isopentenyl diphosphate (By similarity). FT BINDING 109 109 Dimethylallyl diphosphate (By FT similarity). FT BINDING 110 110 Isopentenyl diphosphate (By similarity). FT BINDING 197 197 Dimethylallyl diphosphate (By FT similarity). FT BINDING 198 198 Dimethylallyl diphosphate (By FT similarity). FT BINDING 237 237 Dimethylallyl diphosphate (By FT similarity). FT BINDING 254 254 Dimethylallyl diphosphate (By FT similarity). FT BINDING 263 263 Dimethylallyl diphosphate (By FT similarity). FT MUTAGEN 197 197 K->E: In ERG20-2; 14-fold decrease in FT FPPS activity. SQ SEQUENCE 352 AA; 40483 MW; 79A357BB7BFCEDDA CRC64; MASEKEIRRE RFLNVFPKLV EELNASLLAY GMPKEACDWY AHSLNYNTPG GKLNRGLSVV DTYAILSNKT VEQLGQEEYE KVAILGWCIE LLQAYFLVAD DMMDKSITRR GQPCWYKVPE VGEIAINDAF MLEAAIYKLL KSHFRNEKYY IDITELFHEV TFQTELGQLM DLITAPEDKV DLSKFSLKKH SFIVTFKTAY YSFYLPVALA MYVAGITDEK DLKQARDVLI PLGEYFQIQD DYLDCFGTPE QIGKIGTDIQ DNKCSWVINK ALELASAEQR KTLDENYGKK DSVAEAKCKK IFNDLKIEQL YHEYEESIAK DLKAKISQVD ESRGFKADVL TAFLNKVYKR SK //