ID   GGPPS_NEUCR             Reviewed;         433 AA.
AC   P24322; Q7RVC0; Q86ZV1;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-NOV-2008, entry version 76.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthetase;
DE            Short=GGPP synthetase;
DE            Short=GGPPSase;
DE   AltName: Full=Geranylgeranyl diphosphate synthase;
DE   AltName: Full=Albino-3 protein;
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=al-3; ORFNames=B8P8.010, NCU01427;
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=91170267; PubMed=1826006;
RA   Carattoli A., Romano N., Ballario P., Morelli G., Macino G.;
RT   "The Neurospora crassa carotenoid biosynthetic gene (albino 3) reveals
RT   highly conserved regions among prenyltransferases.";
RL   J. Biol. Chem. 266:5854-5859(1991).
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134, AND ALTERNATIVE
RP   INITIATION.
RX   MEDLINE=95014519; PubMed=7929398;
RA   Vittorioso P., Carattoli A., Londei P., Macino G.;
RT   "Internal translational initiation in the mRNA from the Neurospora
RT   crassa albino-3 gene.";
RL   J. Biol. Chem. 269:26650-26654(1994).
CC   -!- FUNCTION: Catalyzes the trans-addition of the three molecules of
CC       IPP onto DMAPP to form geranylgeranyl 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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=3;
CC       Name=1;
CC         IsoId=P24322-1; Sequence=Displayed;
CC         Note=Main product;
CC       Name=2;
CC         IsoId=P24322-2; Sequence=VSP_029974;
CC       Name=3;
CC         IsoId=P24322-3; Sequence=VSP_029973;
CC   -!- INDUCTION: By blue light.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
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DR   EMBL; U20940; AAC13867.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX294018; CAD70868.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AABX02000014; EAA31459.2; -; Genomic_DNA.
DR   EMBL; S74011; AAP21085.1; -; Genomic_DNA.
DR   PIR; S15662; S15662.
DR   RefSeq; XP_960695.2; -.
DR   GeneID; 3876842; -.
DR   KEGG; ncr:NCU01427; -.
DR   NMPDR; fig|5141.1.peg.4853; -.
DR   BioCyc; NCRA-XX3-01:NCRA-XX3-01-005137-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005625; C:soluble fraction; ISS:UniProtKB.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; ISS:UniProtKB.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR017446; Polyprenyl_synth-rel.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1.
DR   PANTHER; PTHR12001; Polyprenyl_synt; 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   Alternative initiation; Carotenoid biosynthesis; Complete proteome;
KW   Cytoplasm; Isoprene biosynthesis; Multifunctional enzyme; Transferase.
FT   CHAIN         1    433       Geranylgeranyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123966.
FT   ACT_SITE    273    273       By similarity.
FT   VAR_SEQ       1     98       Missing (in isoform 3).
FT                                /FTId=VSP_029973.
FT   VAR_SEQ       1     88       Missing (in isoform 2).
FT                                /FTId=VSP_029974.
SQ   SEQUENCE   433 AA;  48485 MW;  BE6BB03A938BDFA5 CRC64;
     MEHVTMAVTS SSPGPAPLSL LSNNDDFIAP FNINTKFPSA IVPPRTSSNQ PISVAIPSNR
     ISSAGLAATQ QAQTRKRKAS VAQISLPSML PTSFSPYTMA PQPPQPPPNP DRFATEDFFS
     PSRRTWSEEK EKVLTGPYDY LNGHPGKDIR SQMVKAFDAW LDVPSESLEV ITKVISMLHT
     ASLLVDDVED NSVLRRGFPV AHSIFGIPQT INTSNYVYFY ALQELQKLKN PKAVSIFSEE
     LLNLHRGQGM DLFWRDTLTC PTEDDYLEMV SNKTGGLFRL GIKLMQAESR SPVDCVPLVN
     IIGLIFQIAD DYHNLWNREY TANKGMCEDL TEGKFSFPVI HSIRSNPSNM QLLNILKQKT
     GDEEVKRYAV AYMESTGSFE YTRKVIKVLV DRARQMTEDI DDGRGKSGGI HKILDRIMLH
     QEENVAQKNG KKE
//