ID   FPPS2_PARAR             Reviewed;         342 AA.
AC   O24242;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 49.
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   Parthenium argentatum (Guayule rubber plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae; Parthenium.
OX   NCBI_TaxID=35935;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Line 11591; TISSUE=Stem bark;
RX   MEDLINE=96400350; PubMed=8806726; DOI=10.1006/abbi.1996.0333;
RA   Pan Z., Herickhoff L.A., Backhaus R.A.;
RT   "Cloning, characterization, and heterologous expression of cDNAs for
RT   farnesyl diphosphate synthase from the guayule rubber plant reveals
RT   that this prenyltransferase occurs in rubber particles.";
RL   Arch. Biochem. Biophys. 332:196-204(1996).
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. Note=Rubber particles.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; X82543; CAA57893.1; -; mRNA.
DR   PIR; S71399; S71399.
DR   HSSP; P08836; 1UBY.
DR   BRENDA; 2.5.1.1; 268459.
DR   BRENDA; 2.5.1.10; 268459.
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_0000123960.
SQ   SEQUENCE   342 AA;  39385 MW;  3BB216D0D9F99A22 CRC64;
     MSTDIRSKFL QVYDTLKSEL INDPAFEFDD DSRQWIEKML DYNVPGGKLN RGLSVIDSYQ
     LLKGGKLTDD EIFHASALGW CVEWLQAYFL VLDDIMDESH TRRGQPCWFR LPKVGMIAAN
     DGIILRNHVP RILKKHFRGK PYYVDLVDLF NEVEFQTASG QMIDLITTLV GEKDLSKYSL
     SIHRRIVQYK TAYYSFYLPV ACALLMFGED LEKHVEVKNV LVEMGTYFQV QDDYLDCFGA
     PEVIGKIGTD IEDFKCSWLV VKALELANEE QKKVLHENYG KKDPSPVAKV KELYNTLNLQ
     GVFEDYENTS YKKLITSIEG HPSKAVQAVL KSFLGKIYRR QK
//