ID   FPPS_NEUCR              Reviewed;         347 AA.
AC   Q92250; Q1K859; Q8X0Y6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   16-JUN-2009, entry version 55.
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=fpp; Synonyms=fpps; ORFNames=123A4.020, NCU01175;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; X96944; CAA65645.1; -; Genomic_DNA.
DR   EMBL; AL670009; CAD21355.1; -; Genomic_DNA.
DR   EMBL; AABX02000015; EAA32305.1; -; Genomic_DNA.
DR   PIR; S71436; S71436.
DR   RefSeq; XP_961541.1; -.
DR   HSSP; P08836; 1UBX.
DR   GeneID; 3877737; -.
DR   KEGG; ncr:NCU01175; -.
DR   NMPDR; fig|5141.1.peg.4601; -.
DR   BRENDA; 2.5.1.1; 266.
DR   BRENDA; 2.5.1.10; 266.
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    347       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123950.
FT   ACT_SITE    184    184       By similarity.
FT   CONFLICT    134    134       L -> R (in Ref. 1; CAA65645).
FT   CONFLICT    321    321       I -> N (in Ref. 1; CAA65645).
SQ   SEQUENCE   347 AA;  40278 MW;  83F4DC7C4D61212F CRC64;
     MAKTTTLKEF ESVFPKLEEA LLEYAKAYKL PEQMLSWYKQ SLEVNTLGGK CNRGMSVPDS
     ASILLGRPLT EEEYFQAATL GWMTELLQAF FLVSDDIMDS SITRRGKPCW YRQEGVGMVA
     INDAFMLESA IYTLLKKYFR SHPRYVDFLE LFHEVTFQTE MGQLCDLLTA PEDKVDLDNF
     SMDKYTFIVI YKTAYYSFYL PVALAMYMLD IATPENLKQA EDILIPLGEY FQVQDDYLDN
     FGLPEHIGKI GTDIQDNKCS WLVNKALSIV TPEQRKTLEE NYGRKDKAKE AVIKQLYDDL
     KLEDHYKQYE EERVGEIRKM IDAIDESKGL KKQVFEAFLG KIYKRSK
//