GGPP1_ARATH
ID GGPP1_ARATH Reviewed; 371 AA.
AC P34802; O23201;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic;
DE Short=GGPP synthase 1;
DE Short=GGPS1;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 1;
DE AltName: Full=Dimethylallyltranstransferase 1;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 1;
DE AltName: Full=Farnesyltranstransferase 1;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase 1;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN Name=GGPPS1; Synonyms=GGPPS11, GGPS1; OrderedLocusNames=At4g36810;
GN ORFNames=C7A10.550;
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 [MRNA].
RX PubMed=8016276; DOI=10.1104/pp.104.4.1469;
RA Scolnik P.A., Bartley G.E.;
RT "Nucleotide sequence of an Arabidopsis cDNA for geranylgeranyl
RT pyrophosphate synthase.";
RL Plant Physiol. 104:1469-1470(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX 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 organs
RT are localized into three subcellular compartments in Arabidopsis.";
RL Plant Physiol. 122:1045-1056(2000).
RN [6]
RP FUNCTION, SUBUNIT, AND 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-52, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase
CC large subunit. In vitro, the large subunit catalyzes mainly the trans-
CC addition of the three molecules of IPP onto DMAPP to form
CC geranylgeranyl pyrophosphate while the small subunit alone is inactive.
CC Upon association of the two subunits, the product profile changes and
CC the production of gerany-diphosphate is strongly increased.
CC {ECO:0000269|PubMed:19482937}.
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. Part of a heterodimeric geranyl(geranyl)diphosphate
CC synthase. Interacts with GGR. {ECO:0000269|PubMed:19482937}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10759500}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:10759500}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; L25813; AAA32797.1; -; mRNA.
DR EMBL; Z99708; CAB16803.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80347.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86705.1; -; Genomic_DNA.
DR PIR; F85434; F85434.
DR RefSeq; NP_195399.1; NM_119845.3.
DR PDB; 5E8L; X-ray; 2.81 A; A/B=72-371.
DR PDBsum; 5E8L; -.
DR AlphaFoldDB; P34802; -.
DR SMR; P34802; -.
DR BioGRID; 15115; 3.
DR STRING; 3702.AT4G36810.1; -.
DR iPTMnet; P34802; -.
DR PaxDb; P34802; -.
DR PRIDE; P34802; -.
DR ProteomicsDB; 220742; -.
DR EnsemblPlants; AT4G36810.1; AT4G36810.1; AT4G36810.
DR GeneID; 829834; -.
DR Gramene; AT4G36810.1; AT4G36810.1; AT4G36810.
DR KEGG; ath:AT4G36810; -.
DR Araport; AT4G36810; -.
DR TAIR; locus:2115450; AT4G36810.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; P34802; -.
DR OMA; AWAEFGY; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; P34802; -.
DR BioCyc; ARA:AT4G36810-MON; -.
DR BioCyc; MetaCyc:AT4G36810-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:P34802; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P34802; differential.
DR Genevisible; P34802; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009513; C:etioplast; IDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:TAIR.
DR GO; GO:0004311; F:farnesyltranstransferase 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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 GO; GO:0008299; P:isoprenoid biosynthetic process; TAS:TAIR.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IMP:TAIR.
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 3D-structure; Acetylation; Carotenoid biosynthesis; Chloroplast;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 52..371
FT /note="Heterodimeric geranylgeranyl pyrophosphate synthase
FT large subunit 1, chloroplastic"
FT /id="PRO_0000016471"
FT BINDING 116
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 119
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 148
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 166
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 256
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT MOD_RES 52
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 108
FT /note="R -> S (in Ref. 1; AAA32797)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="A -> R (in Ref. 1; AAA32797)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> S (in Ref. 1; AAA32797)"
FT /evidence="ECO:0000305"
FT HELIX 76..94
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5E8L"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 178..199
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 207..221
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 276..301
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 330..346
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:5E8L"
FT TURN 353..356
FT /evidence="ECO:0007829|PDB:5E8L"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:5E8L"
SQ SEQUENCE 371 AA; 40174 MW; EFA8088A75B6A005 CRC64;
MASVTLGSWI VVHHHNHHHP SSILTKSRSR SCPITLTKPI SFRSKRTVSS SSSIVSSSVV
TKEDNLRQSE PSSFDFMSYI ITKAELVNKA LDSAVPLREP LKIHEAMRYS LLAGGKRVRP
VLCIAACELV GGEESTAMPA ACAVEMIHTM SLIHDDLPCM DNDDLRRGKP TNHKVFGEDV
AVLAGDALLS FAFEHLASAT SSDVVSPVRV VRAVGELAKA IGTEGLVAGQ VVDISSEGLD
LNDVGLEHLE FIHLHKTAAL LEASAVLGAI VGGGSDDEIE RLRKFARCIG LLFQVVDDIL
DVTKSSKELG KTAGKDLIAD KLTYPKIMGL EKSREFAEKL NREARDQLLG FDSDKVAPLL
ALANYIAYRQ N
