ID   FPPS_SCHPO              Reviewed;         347 AA.
AC   O14230; P78756;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
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=fps1; ORFNames=SPAC6F12.13c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-347.
RC   STRAIN=PR745;
RX   MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   FUNCTION, INTERACTION WITH SPO9, AND MUTAGENESIS OF PHE-90 AND
RP   ARG-104.
RX   PubMed=17596513; DOI=10.1091/mbc.E07-02-0112;
RA   Ye Y., Fujii M., Hirata A., Kawamukai M., Shimoda C., Nakamura T.;
RT   "Geranylgeranyl diphosphate synthase in fission yeast is a heteromer
RT   of farnesyl diphosphate synthase (FPS), Fps1, and an FPS-like protein,
RT   Spo9, essential for sporulation.";
RL   Mol. Biol. Cell 18:3568-3581(2007).
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   -!- SUBUNIT: Interacts with spo9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; CU329670; CAB11097.1; -; Genomic_DNA.
DR   EMBL; D89104; BAA13767.1; -; mRNA.
DR   PIR; T11664; T11664.
DR   PIR; T42081; T42081.
DR   RefSeq; NP_593299.1; -.
DR   HSSP; P08836; 1FPS.
DR   GeneID; 2542898; -.
DR   KEGG; spo:SPAC6F12.13c; -.
DR   NMPDR; fig|4896.1.peg.3269; -.
DR   GeneDB_Spombe; SPAC6F12.13c; -.
DR   OMA; O14230; CYGDPAV.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000998-MON; -.
DR   BRENDA; 2.5.1.1; 653.
DR   BRENDA; 2.5.1.10; 653.
DR   ArrayExpress; O14230; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IGI:GeneDB_SPombe.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:GeneDB_SPombe.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IGI:GeneDB_SPombe.
DR   GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IGI:GeneDB_SPombe.
DR   GO; GO:0018342; P:protein prenylation; IC:GeneDB_SPombe.
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   1: Evidence at protein level;
KW   Cholesterol biosynthesis; Complete proteome; Cytoplasm;
KW   Isoprene biosynthesis; Lipid synthesis; Nucleus; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
FT   CHAIN         1    347       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123951.
FT   ACT_SITE    184    184       By similarity.
FT   MUTAGEN      90     90       F->C: Complements lethality of fps1-
FT                                delete strain.
FT   MUTAGEN     104    104       R->Q: No affect on GGPP synthetase
FT                                activity.
FT   CONFLICT    203    203       A -> E (in Ref. 2; BAA13767).
FT   CONFLICT    346    347       NK -> ISKFLVLCF (in Ref. 2; BAA13767).
SQ   SEQUENCE   347 AA;  39516 MW;  483029A5FC15B9F5 CRC64;
     MSAVDKRAKF ESALPVFVDE IVNYLKTINI PDDVTEWYKN SLFHNTLGGK YNRGLSVIDS
     YEILLGHPLD EAAYMKAAVL GWMVELLQSF FLIADDIMDA SKTRRGQPCW YLMPGVGNIA
     INDAFMVESA IYFLLKKHFR QESCYVDLIE LFHDVTFQTE LGQQLDLLTA PEDSVDLSKF
     SLQKHSFIVI YKTAFYSFYL PVALAMHLAG VATPENLKCA QDILIILGKY FQVQDDYLDC
     YGDPTVTGKI GTDILDNKCS WIINLALAKC TPEQRVILDD NYGRKDSESE KRVKAVFEEL
     NIRGEFENYE ESEVSEIKKL IDGVDESTGL KKSIFTTFLG KIYKRNK
//