ID   FPPS_KLULA              Reviewed;         349 AA.
AC   P49349;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 61.
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=FPS1; Synonyms=FPS; OrderedLocusNames=KLLA0A06732g;
OS   Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   MEDLINE=95035105; PubMed=7948032; DOI=10.1016/0167-4781(94)90234-8;
RA   Mulder W., Scholten I.H.J.M., Nagelkerken B., Grivell L.A.;
RT   "Isolation and characterisation of the linked genes, FPS1 and QCR8,
RT   coding for farnesyl-diphosphate synthase and the 11 kDa subunit VIII
RT   of the mitochondrial bc1-complex in the yeast Kluyveromyces lactis.";
RL   Biochim. Biophys. Acta 1219:713-718(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; X76026; CAA53614.1; -; Genomic_DNA.
DR   EMBL; CR382121; CAH02888.1; -; Genomic_DNA.
DR   PIR; S50214; S50214.
DR   RefSeq; XP_451300.1; -.
DR   HSSP; P08836; 1UBY.
DR   GeneID; 2896751; -.
DR   KEGG; kla:KLLA0A06732g; -.
DR   HOGENOM; P49349; -.
DR   OMA; P49349; LVEDDIM.
DR   BRENDA; 2.5.1.1; 74088.
DR   BRENDA; 2.5.1.10; 74088.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cholesterol biosynthesis; Complete proteome; Cytoplasm;
KW   Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
FT   CHAIN         1    349       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123949.
FT   ACT_SITE    186    186       By similarity.
SQ   SEQUENCE   349 AA;  40157 MW;  290557C17FAACDCE CRC64;
     MSDNRAQFLE VFPSLVQELR DILAGYGMPE EAIEWYEKSL NYNTPGGKLN RGLSVVDTYA
     LLKGYKSVSE LSAEEYKKVA ILGWCIELLQ AYFLVADDMM DQSITRRGQP CWYKVENVGD
     IAINDAFMLE GAIYCLLKKH FRTEPYYVDL LELFHDVTFQ TELGQLLDLI TAPEDKVDLS
     KFSLEKHSFI VIFKTAYYSF YLAVALAMFA AGITDSKDLK QASDVLIPLG EYFQIQDDFL
     DCFGKPEDIG KIGTDIQDNK CSWVINVALK NATKEQRDIL DENYGRKDSE KEQKCRAVFN
     ELNIQDIYHK YEEETASNLR EKIANIDESR GFKAEVLTLF LNKIYHRKK
//