ID   GGPPS_SCHPO             Reviewed;         351 AA.
AC   O59703;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 45.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthetase;
DE            Short=GGPP synthetase;
DE            Short=GGPPSase;
DE   AltName: Full=Geranylgeranyl diphosphate synthase;
DE   AltName: Full=Sporulation-specific protein 9;
DE   Includes:
DE     RecName: Full=Dimethylallyltranstransferase;
DE              EC=2.5.1.1;
DE   Includes:
DE     RecName: Full=Geranyltranstransferase;
DE              EC=2.5.1.10;
DE   Includes:
DE     RecName: Full=Farnesyltranstransferase;
DE              EC=2.5.1.29;
GN   Name=spo9; ORFNames=SPBC36.06c;
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   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   [3]
RP   FUNCTION, INTERACTION WITH FPS1, AND MUTAGENESIS OF CYS-95 AND
RP   ARG-109.
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 trans-addition of the 3 molecules of IPP
CC       onto DMAPP to form geranylgeranyl pyrophosphate. Required for the
CC       membrane attachment of ypt7 and rhb1. May be involved in vesicle
CC       trafficking and protein sorting. Required for forespore membrane
CC       formation.
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   -!- CATALYTIC ACTIVITY: Trans,trans-farnesyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranylgeranyl 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   -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl-PP biosynthesis;
CC       geranylgeranyl-PP from farnesyl-PP and isopentenyl-PP: step 1/1.
CC   -!- SUBUNIT: Interacts with fps1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; CU329671; CAA19054.1; -; Genomic_DNA.
DR   PIR; T40301; T40301.
DR   RefSeq; NP_595334.1; -.
DR   HSSP; P08836; 1FPS.
DR   GeneID; 2540933; -.
DR   KEGG; spo:SPBC36.06c; -.
DR   NMPDR; fig|4896.1.peg.1200; -.
DR   GeneDB_Spombe; SPBC36.06c; -.
DR   OMA; O59703; MELANEN.
DR   ArrayExpress; O59703; -.
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; IEA:EC.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:GeneDB_SPombe.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; IMP:GeneDB_SPombe.
DR   GO; GO:0030437; P:ascospore formation; IMP:GeneDB_SPombe.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0018342; P:protein prenylation; IMP:GeneDB_SPombe.
DR   GO; GO:0015031; P:protein transport; 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   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Complete proteome; Cytoplasm;
KW   Isoprene biosynthesis; Multifunctional enzyme; Nucleus;
KW   Protein transport; Transferase; Transport.
FT   CHAIN         1    351       Geranylgeranyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000339411.
FT   MUTAGEN      95     95       C->F: No complement of lethality of fps1-
FT                                delete strain.
FT   MUTAGEN     109    109       R->Q: No GGPP synthetase activity.
SQ   SEQUENCE   351 AA;  40946 MW;  F5DC90A91CC132E7 CRC64;
     MVNDFNEKNG IKKRLLDFFP VVLEGIREIL ESMQYFPEET EKLLYSIKRN TLGGKNNRGL
     AVLQSLTSLI NRELEEAEFR DAALLGWLIE ILQGCFLMAD DIMDQSIKRR GLDCWYLVVG
     VRRAINESQL LEACIPLLIR KYFRNMPYYV DLLDTFREVT FLTELGQQED LLSSRDGEAS
     LRSFDLMKYD FIITYKTSFY SFYLPIKCAL LLSRNSNQKA YDTTIKLSKL LGYYFQVQDD
     YLDCFGDYTV LGKVGMDIQD NKCTWLVCYA EKFASADQLN LLRAHYGKAG SENIAVIKQL
     YHELQIPELY HKFEDDMVDS ISKEIDLIDE STGLKKCIFT KFFQLIYKRS R
//