ID   FPPS_YEAST              Reviewed;         352 AA.
AC   P08524; P15495;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   22-JUL-2008, entry version 79.
DE   RecName: Full=Farnesyl pyrophosphate synthetase;
DE            Short=FPP synthetase;
DE            Short=FPS;
DE   AltName: Full=Farnesyl diphosphate synthetase;
DE   Includes:
DE     RecName: Full=Dimethylallyltranstransferase;
DE              EC=2.5.1.1;
DE   Includes:
DE     RecName: Full=Geranyltranstransferase;
DE              EC=2.5.1.10;
GN   Name=FPP1; Synonyms=BOT3, ERG20, FDS1; OrderedLocusNames=YJL167W;
GN   ORFNames=J0525;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-352.
RX   MEDLINE=87246620; PubMed=3036507;
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   [4]
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 + trans,trans-farnesyl diphosphate.
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis;
CC       farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis;
CC       geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1.
CC   -!- INTERACTION:
CC       Q08409:AUS1; NbExp=1; IntAct=EBI-7069, EBI-35723;
CC       P40318:SSM4; NbExp=1; IntAct=EBI-7069, EBI-18208;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; J05091; AAA34606.1; -; Genomic_DNA.
DR   EMBL; Z49442; CAA89462.1; -; Genomic_DNA.
DR   EMBL; X05550; CAA29064.1; -; Genomic_DNA.
DR   PIR; A34441; A34441.
DR   RefSeq; NP_012368.1; -.
DR   HSSP; P08836; 1FPS.
DR   DIP; DIP:1163N; -.
DR   IntAct; P08524; -.
DR   PeptideAtlas; P08524; -.
DR   Ensembl; YJL167W; Saccharomyces cerevisiae.
DR   GeneID; 853272; -.
DR   GenomeReviews; Y13136_GR; YJL167W.
DR   KEGG; sce:YJL167W; -.
DR   NMPDR; fig|4932.3.peg.3332; -.
DR   CYGD; YJL167w; -.
DR   SGD; S000003703; ERG20.
DR   HOGENOM; P08524; -.
DR   BioCyc; MetaCyc:MON-655; -.
DR   LinkHub; P08524; -.
DR   ArrayExpress; P08524; -.
DR   GermOnline; YJL167W; Saccharomyces cerevisiae.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:SGD.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IDA:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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   Pfam; PF00348; polyprenyl_synt; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1.
PE   1: Evidence at protein level;
KW   Cholesterol biosynthesis; Complete proteome; Cytoplasm;
KW   Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
FT   CHAIN         1    352       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123952.
FT   ACT_SITE    189    189       By 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
//