GGPP9_ARATH
ID GGPP9_ARATH Reviewed; 360 AA.
AC Q9LUE1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase 9, chloroplastic;
DE Short=GGPP synthase 9;
DE Short=GGPS9;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 9;
DE AltName: Full=Dimethylallyltranstransferase 9;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 9;
DE AltName: Full=Farnesyltranstransferase 9;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase 9;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN Name=GGPPS9; Synonyms=GGPPS6; OrderedLocusNames=At3g14530; ORFNames=MIE1.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP LACK OF INTERACTION WITH GGR.
RX PubMed=19482937; DOI=10.1073/pnas.0904069106;
RA Wang G., Dixon R.A.;
RT "Heterodimeric geranyl(geranyl)diphosphate synthase from hop (Humulus
RT lupulus) and the evolution of monoterpene biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9914-9919(2009).
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP
CC onto DMAPP to form geranylgeranyl pyrophosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1.
CC -!- SUBUNIT: Monomer (By similarity). No interactions with GGR.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB023038; BAB02385.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75535.1; -; Genomic_DNA.
DR EMBL; BT010463; AAQ65086.1; -; mRNA.
DR RefSeq; NP_188071.1; NM_112313.3.
DR AlphaFoldDB; Q9LUE1; -.
DR SMR; Q9LUE1; -.
DR STRING; 3702.AT3G14530.1; -.
DR PaxDb; Q9LUE1; -.
DR PRIDE; Q9LUE1; -.
DR ProteomicsDB; 221844; -.
DR EnsemblPlants; AT3G14530.1; AT3G14530.1; AT3G14530.
DR GeneID; 820678; -.
DR Gramene; AT3G14530.1; AT3G14530.1; AT3G14530.
DR KEGG; ath:AT3G14530; -.
DR Araport; AT3G14530; -.
DR TAIR; locus:2089626; AT3G14530.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; Q9LUE1; -.
DR OMA; SYIAGRH; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q9LUE1; -.
DR BioCyc; ARA:AT3G14530-MON; -.
DR BRENDA; 2.5.1.81; 399.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:Q9LUE1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUE1; baseline and differential.
DR Genevisible; Q9LUE1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IDA:TAIR.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
DR GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IDA:TAIR.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IDA:TAIR.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chloroplast; Isoprene biosynthesis; Magnesium;
KW Metal-binding; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..360
FT /note="Geranylgeranyl pyrophosphate synthase 9,
FT chloroplastic"
FT /id="PRO_0000402123"
FT BINDING 106
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 109
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 138
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 156
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 245
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 38673 MW; 95DE35915E52691C CRC64;
MATTVHLSSS SLFSQSRGRR DNSISSVKSL RKRTVLSLSS ALTSQDAGHM IQPEGKSNDN
NSAFDFKLYM IRKAESVNAA LDVSVPLLKP LTIQEAVRYS LLAGGKRVRP LLCIAACELV
GGDEATAMSA ACAVEMIHTS SLIHDDLPCM DNADLRRGKP TNHKVYGEDM AVLAGDALLA
LAFEHMTVVS SGLVAPEKMI RAVVELARAI GTTGLVAGQM IDLASERLNP DKVGLEHLEF
IHLHKTAALL EAAAVLGVIM GGGTEQEIEK LRKYARCIGL LFQVVDDILD VTKSTEELGK
TAGKDVMAGK LTYPRLIGLE GSREVAEKLR REAEEQLLGF DPSKAAPLVA LASYIACRHN
