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Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic (GGPP synthase 1) (GGPS1) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 1) (Dimethylallyltranstransferase 1) (EC 2.5.1.1) (Farnesyl diphosphate synthase 1) (Farnesyltranstransferase 1) (EC 2.5.1.29) (Geranyltranstransferase 1) (EC 2.5.1.10)

 GGPP1_ARATH             Reviewed;         371 AA.
P34802; O23201;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
23-MAY-2018, entry version 140.
RecName: Full=Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic;
Short=GGPP synthase 1;
Short=GGPS1;
EC=2.5.1.-;
AltName: Full=(2E,6E)-farnesyl diphosphate synthase 1;
AltName: Full=Dimethylallyltranstransferase 1;
EC=2.5.1.1;
AltName: Full=Farnesyl diphosphate synthase 1;
AltName: Full=Farnesyltranstransferase 1;
EC=2.5.1.29;
AltName: Full=Geranyltranstransferase 1;
EC=2.5.1.10;
Flags: Precursor;
Name=GGPPS1; Synonyms=GGPPS11, GGPS1; OrderedLocusNames=At4g36810;
ORFNames=C7A10.550;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8016276; DOI=10.1104/pp.104.4.1469;
Scolnik P.A., Bartley G.E.;
"Nucleotide sequence of an Arabidopsis cDNA for geranylgeranyl
pyrophosphate synthase.";
Plant Physiol. 104:1469-1470(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10759500; DOI=10.1104/pp.122.4.1045;
Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y.;
"Five geranylgeranyl diphosphate synthases expressed in different
organs are localized into three subcellular compartments in
Arabidopsis.";
Plant Physiol. 122:1045-1056(2000).
[6]
FUNCTION, SUBUNIT, AND INTERACTION WITH GGR.
PubMed=19482937; DOI=10.1073/pnas.0904069106;
Wang G., Dixon R.A.;
"Heterodimeric geranyl(geranyl)diphosphate synthase from hop (Humulus
lupulus) and the evolution of monoterpene biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 106:9914-9919(2009).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-52, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-51, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Heterodimeric geranyl(geranyl)-diphosphate (GPP)
synthase large subunit. In vitro, the large subunit catalyzes
mainly the trans-addition of the three molecules of IPP onto DMAPP
to form geranylgeranyl pyrophosphate while the small subunit alone
is inactive. Upon association of the two subunits, the product
profile changes and the production of gerany-diphosphate is
strongly increased. {ECO:0000269|PubMed:19482937}.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
diphosphate = diphosphate + geranyl diphosphate.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
= diphosphate + (2E,6E)-farnesyl diphosphate.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + isopentenyl
diphosphate = diphosphate + geranylgeranyl diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
-!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
biosynthesis; farnesyl diphosphate from geranyl diphosphate and
isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- SUBUNIT: Monomer. Part of a heterodimeric
geranyl(geranyl)diphosphate synthase. Interacts with GGR.
{ECO:0000269|PubMed:19482937}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:10759500}.
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:10759500}.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L25813; AAA32797.1; -; mRNA.
EMBL; Z99708; CAB16803.1; -; Genomic_DNA.
EMBL; AL161590; CAB80347.1; -; Genomic_DNA.
EMBL; CP002687; AEE86705.1; -; Genomic_DNA.
PIR; F85434; F85434.
RefSeq; NP_195399.1; NM_119845.3.
UniGene; At.304; -.
PDB; 5E8L; X-ray; 2.81 A; A/B=72-371.
PDBsum; 5E8L; -.
ProteinModelPortal; P34802; -.
SMR; P34802; -.
BioGrid; 15115; 3.
STRING; 3702.AT4G36810.1; -.
iPTMnet; P34802; -.
PaxDb; P34802; -.
PRIDE; P34802; -.
EnsemblPlants; AT4G36810.1; AT4G36810.1; AT4G36810.
GeneID; 829834; -.
Gramene; AT4G36810.1; AT4G36810.1; AT4G36810.
KEGG; ath:AT4G36810; -.
Araport; AT4G36810; -.
TAIR; locus:2115450; AT4G36810.
eggNOG; KOG0776; Eukaryota.
eggNOG; COG0142; LUCA.
HOGENOM; HOG000009101; -.
InParanoid; P34802; -.
KO; K13789; -.
OMA; GRPTLHK; -.
OrthoDB; EOG09360HVD; -.
PhylomeDB; P34802; -.
BioCyc; ARA:AT4G36810-MONOMER; -.
BioCyc; MetaCyc:AT4G36810-MONOMER; -.
UniPathway; UPA00259; UER00368.
UniPathway; UPA00260; UER00369.
UniPathway; UPA00389; UER00564.
PRO; PR:P34802; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P34802; differential.
Genevisible; P34802; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0009513; C:etioplast; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:TAIR.
GO; GO:0004311; F:farnesyltranstransferase activity; IDA:TAIR.
GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008299; P:isoprenoid biosynthetic process; TAS:TAIR.
GO; GO:0043693; P:monoterpene biosynthetic process; IMP:TAIR.
Gene3D; 1.10.600.10; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR000092; Polyprenyl_synt.
InterPro; IPR033749; Polyprenyl_synt_CS.
Pfam; PF00348; polyprenyl_synt; 1.
SUPFAM; SSF48576; SSF48576; 1.
PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Carotenoid biosynthesis; Chloroplast;
Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
Plastid; Reference proteome; Transferase; Transit peptide.
TRANSIT 1 51 Chloroplast.
{ECO:0000244|PubMed:22223895}.
CHAIN 52 371 Heterodimeric geranylgeranyl
pyrophosphate synthase large subunit 1,
chloroplastic.
/FTId=PRO_0000016471.
COMPBIAS 21 58 Ser-rich.
METAL 155 155 Magnesium 1. {ECO:0000250}.
METAL 155 155 Magnesium 2. {ECO:0000250}.
METAL 161 161 Magnesium 1. {ECO:0000250}.
METAL 161 161 Magnesium 2. {ECO:0000250}.
METAL 297 297 Magnesium 3. {ECO:0000250}.
BINDING 116 116 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 119 119 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 148 148 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 166 166 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 167 167 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 256 256 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 257 257 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 294 294 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 311 311 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 321 321 Dimethylallyl diphosphate. {ECO:0000250}.
MOD_RES 52 52 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
CONFLICT 108 108 R -> S (in Ref. 1; AAA32797).
{ECO:0000305}.
CONFLICT 141 141 A -> R (in Ref. 1; AAA32797).
{ECO:0000305}.
CONFLICT 192 192 A -> S (in Ref. 1; AAA32797).
{ECO:0000305}.
HELIX 76 94 {ECO:0000244|PDB:5E8L}.
HELIX 101 111 {ECO:0000244|PDB:5E8L}.
HELIX 118 129 {ECO:0000244|PDB:5E8L}.
TURN 134 137 {ECO:0000244|PDB:5E8L}.
HELIX 138 155 {ECO:0000244|PDB:5E8L}.
TURN 158 161 {ECO:0000244|PDB:5E8L}.
STRAND 164 166 {ECO:0000244|PDB:5E8L}.
HELIX 172 176 {ECO:0000244|PDB:5E8L}.
HELIX 178 199 {ECO:0000244|PDB:5E8L}.
TURN 202 204 {ECO:0000244|PDB:5E8L}.
HELIX 207 221 {ECO:0000244|PDB:5E8L}.
TURN 222 224 {ECO:0000244|PDB:5E8L}.
HELIX 226 232 {ECO:0000244|PDB:5E8L}.
HELIX 246 256 {ECO:0000244|PDB:5E8L}.
HELIX 258 271 {ECO:0000244|PDB:5E8L}.
HELIX 276 301 {ECO:0000244|PDB:5E8L}.
TURN 319 321 {ECO:0000244|PDB:5E8L}.
HELIX 324 328 {ECO:0000244|PDB:5E8L}.
HELIX 330 346 {ECO:0000244|PDB:5E8L}.
TURN 347 350 {ECO:0000244|PDB:5E8L}.
TURN 353 356 {ECO:0000244|PDB:5E8L}.
HELIX 357 368 {ECO:0000244|PDB:5E8L}.
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


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