ID   GGPP6_ARATH             Reviewed;         336 AA.
AC   O22043; Q9XIC0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthetase 6, mitochondrial;
DE            Short=GGPP synthetase 6;
DE            Short=GGPS6;
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=GGPP6; OrderedLocusNames=At1g49530; ORFNames=F13F21.3;
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], AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   MEDLINE=98009970; PubMed=9349257; DOI=10.1023/A:1005898805326;
RA   Zhu X., Suzuki K., Saito T., Okada K., Tanaka K., Nakagawa T.,
RA   Matsuda H., Kawamukai M.;
RT   "Geranylgeranyl pyrophosphate synthase encoded by the newly isolated
RT   gene GGPS6 from Arabidopsis thaliana is localized in mitochondria.";
RL   Plant Mol. Biol. 35:331-341(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; AB000835; BAA23157.1; -; Genomic_DNA.
DR   EMBL; AC007504; AAD43148.1; -; Genomic_DNA.
DR   EMBL; BT011230; AAR92266.1; -; mRNA.
DR   EMBL; BT012158; AAS76253.1; -; mRNA.
DR   IPI; IPI00537288; -.
DR   RefSeq; NP_175376.1; -.
DR   UniGene; At.38214; -.
DR   GeneID; 841377; -.
DR   GenomeReviews; CT485782_GR; AT1G49530.
DR   KEGG; ath:AT1G49530; -.
DR   NMPDR; fig|3702.1.peg.4426; -.
DR   TAIR; At1g49530; -.
DR   BRENDA; 2.5.1.1; 302.
DR   BRENDA; 2.5.1.10; 302.
DR   BRENDA; 2.5.1.29; 302.
DR   GermOnline; AT1G49530; Arabidopsis thaliana.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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; Isoprene biosynthesis;
KW   Mitochondrion; Multifunctional enzyme; Transferase; Transit peptide.
FT   TRANSIT       1     22       Mitochondrion (Potential).
FT   CHAIN        23    336       Geranylgeranyl pyrophosphate synthetase
FT                                6, mitochondrial.
FT                                /FTId=PRO_0000045405.
FT   CONFLICT      1      1       M -> MLCKIIIM (in Ref. 1 and 2).
FT   CONFLICT      4      4       R -> C (in Ref. 1 and 2).
FT   CONFLICT      8      8       I -> V (in Ref. 1 and 2).
FT   CONFLICT     37     37       K -> N (in Ref. 1 and 2).
FT   CONFLICT     57     57       F -> S (in Ref. 1 and 2).
FT   CONFLICT     77     77       P -> S (in Ref. 1 and 2).
FT   CONFLICT    133    133       K -> I (in Ref. 1 and 2).
FT   CONFLICT    153    153       R -> M (in Ref. 1 and 2).
SQ   SEQUENCE   336 AA;  36886 MW;  95F32D360003C954 CRC64;
     MRPRYSLILS AMRLIRPSNR RLSSIASSDS EFISYMKNKA KSINKALDNS IPLCNNFVPL
     WEPVLEVHKA MRYTLLPGGK RVRPMLCLVA CELVGGQEST AMPAACAVEM IHAASLILDD
     LPCMDDDSLR RGKPTNHKVF GEKTSILASN ALRSLAVKQT LASTSLGVTS ERVLRAVQEM
     ARAVGTEGLV AGQAADLAGE RMSFKNEDDE LRYLELMHVH KTAVLVEAAA VVGAIMGGGS
     DEEIERLKSY ARCVGLMFQV MDDVLDETKS SEELGKTAGK DLITGKLTYP KVMGVDNARE
     YAKRLNREAQ EHLQGFDSDK VVPLLSLADY IVKRQN
//