ID   FPPS1_LUPAL             Reviewed;         342 AA.
AC   P49351;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Farnesyl pyrophosphate synthetase 1;
DE            Short=FPP synthetase 1;
DE            Short=FPS 1;
DE   AltName: Full=Farnesyl diphosphate synthetase 1;
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;
OS   Lupinus albus (White lupin).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Genisteae;
OC   Lupinus.
OX   NCBI_TaxID=3870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   MEDLINE=95374057; PubMed=7646076; DOI=10.1006/abbi.1995.1422;
RA   Attucci S., Aitken S.M., Gulick P.J., Ibrahim R.K.;
RT   "Farnesyl pyrophosphate synthase from white lupin: molecular cloning,
RT   expression, and purification of the expressed protein.";
RL   Arch. Biochem. Biophys. 321:493-500(1995).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; U15777; AAA86687.1; -; mRNA.
DR   PIR; S66470; S66470.
DR   HSSP; P08836; 1UBY.
DR   BRENDA; 2.5.1.1; 956.
DR   BRENDA; 2.5.1.10; 956.
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   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Cytoplasm; Isoprene biosynthesis;
KW   Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis;
KW   Transferase.
FT   CHAIN         1    342       Farnesyl pyrophosphate synthetase 1.
FT                                /FTId=PRO_0000123956.
SQ   SEQUENCE   342 AA;  39269 MW;  591DE4CD29CC711C CRC64;
     MADLRSTFLN VYSVLKSELL HDPAFEFSPD SRQWLDRMLD YNVPGGKLNR GLSVIDSYRL
     LKDGHELNDD EIFLASALGW CIEWLQAYFL VLDDIMDNSH TRRGQPCWFR VPKVGMIAAN
     DGVLLRNHIP RILKKHFRGK PYYADLLDLF NEVEFQTASG QMIDLITTLE GEKDLSKYTL
     SLHRRIVQYK TAYYSFYLPV ACALLMVGEN LDNHIDVKNI LVDMGTYFQV QDDYLDCFGA
     PETIGKIGTD IEDFKCSWLV VKALELSNDE QKKVLYDNYG KPDPANVAKV KALYDELNLQ
     GVFTEYESKS YEKLVTSIEA HPSKAVQALL KSFLGKIYKR QK
//