ID   FPPS_GIBFU              Reviewed;         347 AA.
AC   Q92235;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JUN-2009, entry version 47.
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=FPPS;
OS   Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   moniliforme).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella; Gibberella fujikuroi complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=m567;
RX   MEDLINE=96337905; PubMed=8753652; DOI=10.1007/s002940050126;
RA   Homann V., Mende K., Arntz C., Ilardi V., Macino G., Morelli G.,
RA   Bose G., Tudzynski B.;
RT   "The isoprenoid pathway: cloning and characterization of fungal FPPS
RT   genes.";
RL   Curr. Genet. 30:232-239(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.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; X96940; CAA65641.1; -; Genomic_DNA.
DR   PIR; S71435; S71435.
DR   HSSP; P08836; 1UBX.
DR   BRENDA; 2.5.1.1; 97815.
DR   BRENDA; 2.5.1.10; 97815.
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; Cytoplasm; Isoprene biosynthesis;
KW   Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis;
KW   Transferase.
FT   CHAIN         1    347       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123948.
FT   ACT_SITE    184    184       By similarity.
SQ   SEQUENCE   347 AA;  40236 MW;  DC39B016658441E4 CRC64;
     MAQQTTLQEF NSVYPKLEEA LLDHARSYKL PQEQLDWYKR SLEVNPLGGK CNRGMSVPDS
     VSLLLEKPLT EEQYFQAATL GWMTELLQAF FLVSDDIMDS SITRRGQPCW YRQEGVGMIA
     INDAFMLESA IYTLLKKYFR SHPAYFDLIE SFHETTFQTE LGQLCDLLTA PEDNVNLDNF
     SLEKYSFIVI YKTAYYSFYL PVALALHQLN LATPSNLKQA EDILIPLGEY FQIQDDYLDN
     FGKPEHIGKI GTDIKDNKCS WLVNQALAVA TPEQRKILEE NYGRKDDEKE KVVKKLYDDL
     NLEQRYLDYE EKVVGQIRER IANIDENDGL KKTVFEAFLA KIYKRSK
//