ID   FPPS2_LUPAL             Reviewed;         342 AA.
AC   P49352;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Farnesyl pyrophosphate synthetase 2;
DE            Short=FPP synthetase 2;
DE            Short=FPS 2;
DE   AltName: Full=Farnesyl diphosphate synthetase 2;
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=FPS2;
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; U20771; AAA87729.1; -; mRNA.
DR   PIR; S66471; S66471.
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 2.
FT                                /FTId=PRO_0000123957.
SQ   SEQUENCE   342 AA;  39311 MW;  EB2C3AD89626E42D CRC64;
     MADPKSSFLN VYSILKSELL QDPAFEFSTD SRQWVERMLD YNVPGGKLNR GLSVIDSYKL
     LKDGQELNDE EIFLASALGW CIEWLQAYFL VLDDIMDNSH TRRGHPCWFR VPKVGMIAPN
     DGVVLRNHIP RILKKHFRGK PYYVDLLDLF NEVEFQTASG QMIDLITTLE GEKDLSKYTL
     SLHRRIVQYK TAYYSFYLPV ACALLMVGEN LDNHTDVKNI LVEMGTYFQV QDDYLDCFGA
     PETIGKIGTD IEDFKCSWLV VKALELSNEE QKKVLYENYG KPDPANVAKV KTLYNELNLE
     GAYADYESKS YEKLVTCIEG HPSKAVQGVL KSFWAKIYKR QK
//