GGR_ARATH
ID GGR_ARATH Reviewed; 326 AA.
AC Q39108; Q9FPK0; Q9SZM6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Heterodimeric geranylgeranyl pyrophosphate synthase small subunit, chloroplastic;
DE Flags: Precursor;
GN Name=GGR; OrderedLocusNames=At4g38460; ORFNames=F20M13.20;
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].
RC STRAIN=cv. Columbia;
RA Scolnik P.A., Bartley G.E.;
RT "Nucleotide sequence of a putative geranylgeranyl pyrophosphate synthase
RT from Arabidopsis.";
RL (er) Plant Gene Register PGR95-018(1995).
RN [2]
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 [3]
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 [4]
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 [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 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 [7]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH GGPPS1; GGPPS2 AND GGPPS9.
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 [8]
RP INTERACTION WITH LIL3.1 AND LIL3.2.
RX PubMed=20823244; DOI=10.1073/pnas.1004699107;
RA Tanaka R., Rothbart M., Oka S., Takabayashi A., Takahashi K., Shibata M.,
RA Myouga F., Motohashi R., Shinozaki K., Grimm B., Tanaka A.;
RT "LIL3, a light-harvesting-like protein, plays an essential role in
RT chlorophyll and tocopherol biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16721-16725(2010).
CC -!- FUNCTION: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase
CC small subunit. The small subunit alone is inactive in vitro while the
CC large subunit GGPPS1 catalyzes mainly the production of geranygeranyl-
CC diphosphate in vitro. Upon association of the two subunits, the product
CC profile changes and the production of gerany-diphosphate is strongly
CC increased. {ECO:0000269|PubMed:19482937}.
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 -!- SUBUNIT: Part of a heterodimeric geranyl(geranyl)diphosphate synthase.
CC Interacts with GGPPS1 or GGPPS2, but not with GGPPS9 (PubMed:19482937).
CC Interacts with LIL3.1 and LIL3.2 (PubMed:20823244).
CC {ECO:0000269|PubMed:19482937, ECO:0000269|PubMed:20823244}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
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; L40577; AAA81879.1; -; mRNA.
DR EMBL; AL035540; CAB37502.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80510.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86930.1; -; Genomic_DNA.
DR EMBL; AY057734; AAL15364.1; -; mRNA.
DR EMBL; AF324662; AAG40013.1; -; mRNA.
DR EMBL; AF326906; AAG41488.1; -; mRNA.
DR EMBL; AF339725; AAK00407.1; -; mRNA.
DR EMBL; AF372915; AAK49631.1; -; mRNA.
DR EMBL; AY086829; AAM63877.1; -; mRNA.
DR PIR; T05674; T05674.
DR RefSeq; NP_195558.1; NM_120007.4.
DR AlphaFoldDB; Q39108; -.
DR SMR; Q39108; -.
DR BioGRID; 15282; 3.
DR IntAct; Q39108; 1.
DR STRING; 3702.AT4G38460.1; -.
DR PaxDb; Q39108; -.
DR PRIDE; Q39108; -.
DR ProteomicsDB; 224787; -.
DR EnsemblPlants; AT4G38460.1; AT4G38460.1; AT4G38460.
DR GeneID; 830002; -.
DR Gramene; AT4G38460.1; AT4G38460.1; AT4G38460.
DR KEGG; ath:AT4G38460; -.
DR Araport; AT4G38460; -.
DR TAIR; locus:2121149; AT4G38460.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; Q39108; -.
DR OMA; VEMVHAA; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q39108; -.
DR PRO; PR:Q39108; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39108; baseline and differential.
DR Genevisible; Q39108; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IMP:TAIR.
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.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Magnesium; Membrane; Metal-binding; Plastid;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..33
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 34..326
FT /note="Heterodimeric geranylgeranyl pyrophosphate synthase
FT small subunit, chloroplastic"
FT /id="PRO_0000045406"
FT COILED 274..301
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 120
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 138
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 220
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT CONFLICT 84
FT /note="A -> P (in Ref. 1; AAA81879)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="A -> P (in Ref. 1; AAA81879)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="A -> E (in Ref. 4; AAG40013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35189 MW; 89494E00740CD475 CRC64;
MLFSGSAIPL SSFCSLPEKP HTLPMKLSPA AIRSSSSSAP GSLNFDLRTY WTTLITEINQ
KLDEAIPVKH PAGIYEAMRY SVLAQGAKRA PPVMCVAACE LFGGDRLAAF PTACALEMVH
AASLIHDDLP CMDDDPVRRG KPSNHTVYGS GMAILAGDAL FPLAFQHIVS HTPPDLVPRA
TILRLITEIA RTVGSTGMAA GQYVDLEGGP FPLSFVQEKK FGAMGECSAV CGGLLGGATE
DELQSLRRYG RAVGMLYQVV DDITEDKKKS YDGGAEKGMM EMAEELKEKA KKELQVFDNK
YGGGDTLVPL YTFVDYAAHR HFLLPL
