ID   GGPP2_ARATH             Reviewed;         376 AA.
AC   O04046; Q38917; Q7DN59;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthetase 2;
DE            Short=GGPP synthetase 2;
DE            Short=GGPS2;
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;
DE   Flags: Precursor;
GN   Name=GGPP2; Synonyms=GGPP5; OrderedLocusNames=At2g23800;
GN   ORFNames=F27L4.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RA   Scolnik P.A., Bartley G.E.;
RT   "Two more members of an Arabidopsis geranylgeranyl pyrophosphate
RT   synthase gene family.";
RL   (er) Plant Gene Register PGR96-014.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21932900; PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-376.
RX   MEDLINE=97294934; PubMed=9150607;
RA   Zhu X.F., Suzuki K., Okada K., Tanaka K., Nakagawa T., Kawamukai M.,
RA   Matsuda K.;
RT   "Cloning and functional expression of a novel geranylgeranyl
RT   pyrophosphate synthase gene from Arabidopsis thaliana in Escherichia
RT   coli.";
RL   Plant Cell Physiol. 38:357-361(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-376, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=20223719; PubMed=10759500; DOI=10.1104/pp.122.4.1045;
RA   Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y.;
RT   "Five geranylgeranyl diphosphate synthases expressed in different
RT   organs are localized into three subcellular compartments in
RT   Arabidopsis.";
RL   Plant Physiol. 122:1045-1056(2000).
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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in flowers.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB67730.1; Type=Frameshift; Positions=5;
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DR   EMBL; U44876; AAB67730.1; ALT_FRAME; mRNA.
DR   EMBL; AC004482; AAC17083.1; -; Genomic_DNA.
DR   EMBL; BT005328; AAO63392.1; -; mRNA.
DR   EMBL; AK117954; BAC42592.1; -; mRNA.
DR   EMBL; AY087521; AAM65063.1; -; mRNA.
DR   EMBL; D85029; BAA19583.1; -; mRNA.
DR   IPI; IPI00535829; -.
DR   PIR; S71230; S71230.
DR   PIR; T02429; T02429.
DR   RefSeq; NP_179960.1; -.
DR   UniGene; At.1550; -.
DR   SMR; O04046; 86-371.
DR   PRIDE; O04046; -.
DR   GeneID; 816912; -.
DR   GenomeReviews; CT485783_GR; AT2G23800.
DR   KEGG; ath:AT2G23800; -.
DR   NMPDR; fig|3702.1.peg.9405; -.
DR   TAIR; At2g23800; -.
DR   OMA; O04046; ISSERMV.
DR   BioCyc; MetaCyc:AT2G23800-MON; -.
DR   BRENDA; 2.5.1.1; 302.
DR   BRENDA; 2.5.1.10; 302.
DR   BRENDA; 2.5.1.29; 302.
DR   ArrayExpress; O04046; -.
DR   GermOnline; AT2G23800; Arabidopsis thaliana.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IDA:TAIR.
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   Carotenoid biosynthesis; Complete proteome; Endoplasmic reticulum;
KW   Isoprene biosynthesis; Membrane; Multifunctional enzyme; Signal;
KW   Transferase; Transmembrane.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    376       Geranylgeranyl pyrophosphate synthetase
FT                                2.
FT                                /FTId=PRO_0000045402.
FT   TRANSMEM    188    208       Potential.
FT   COMPBIAS     60     72       Poly-Glu.
FT   CONFLICT    146    147       AM -> TI (in Ref. 1; AAB67730).
FT   CONFLICT    182    182       H -> D (in Ref. 1; AAB67730).
SQ   SEQUENCE   376 AA;  41339 MW;  1B643EC4086BD43B CRC64;
     MEPQILFLYL SLFILSLNFF FTNLKPRLVR LFQPSLESRV KTALLSRKEV AAFLDSPIVE
     DEEGEEREEE EEGGIVSNAN FTFEFDPYMM SKAESVNKAL EEAIPVGEPL KIHEAMRYAI
     LAAGKRVRPI LCLASCELVG GQENAAMPAA CAVEMIHTMS LIKDDLPCMD NDDLRRGKPT
     THKVYGEGVA ILSGGALLSL AFEHMTTAEI SSERMVWAVR ELARSIGTRG LVAGQAMDIS
     SEGLDLNEVG LEHLEFIHVH KTAVLLETAA VLGAIIGGGS DEEIESVRKF ARCIGLLFQV
     VDDILDETKS SEELGKTAGK DQLAGKLTYP KLIGLEKSKE FVKRLTKDAR QHLQGFSSEK
     VAPLVALTTF IANRNK
//