GGPP2_ARATH
ID GGPP2_ARATH Reviewed; 376 AA.
AC O04046; Q38917; Q7DN59;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2;
DE Short=GGPP synthase 2;
DE Short=GGPS2;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 2;
DE AltName: Full=Dimethylallyltranstransferase 2;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 2;
DE AltName: Full=Farnesyltranstransferase 2;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase 2;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN Name=GGPPS2; Synonyms=GGPP5, GGPS2; OrderedLocusNames=At2g23800;
GN ORFNames=F27L4.2;
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. Landsberg erecta; TISSUE=Flower;
RA Scolnik P.A., Bartley G.E.;
RT "Two more members of an Arabidopsis geranylgeranyl pyrophosphate synthase
RT gene family.";
RL (er) Plant Gene Register PGR96-014(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-376.
RX PubMed=9150607; DOI=10.1093/oxfordjournals.pcp.a029174;
RA Zhu X.F., Suzuki K., Okada K., Tanaka K., Nakagawa T., Kawamukai M.,
RA Matsuda K.;
RT "Cloning and functional expression of a novel geranylgeranyl pyrophosphate
RT synthase gene from Arabidopsis thaliana in Escherichia coli.";
RL Plant Cell Physiol. 38:357-361(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-376, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
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 [9]
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).
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 is not
CC changed. {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 (By similarity). Part of a heterodimeric
CC geranyl(geranyl)diphosphate synthase. Interacts with GGR. {ECO:0000250,
CC ECO:0000269|PubMed:19482937}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:10759500}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in flowers.
CC {ECO:0000269|PubMed:10759500}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67730.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U44876; AAB67730.1; ALT_FRAME; mRNA.
DR EMBL; AC004482; AAC17083.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07492.1; -; Genomic_DNA.
DR EMBL; BT005328; AAO63392.1; -; mRNA.
DR EMBL; AK117954; BAC42592.1; -; mRNA.
DR EMBL; AY087521; AAM65063.1; -; mRNA.
DR EMBL; D85029; BAA19583.1; -; mRNA.
DR PIR; S71230; S71230.
DR PIR; T02429; T02429.
DR RefSeq; NP_179960.1; NM_127943.3.
DR AlphaFoldDB; O04046; -.
DR SMR; O04046; -.
DR STRING; 3702.AT2G23800.1; -.
DR PaxDb; O04046; -.
DR PRIDE; O04046; -.
DR ProteomicsDB; 220743; -.
DR EnsemblPlants; AT2G23800.1; AT2G23800.1; AT2G23800.
DR GeneID; 816912; -.
DR Gramene; AT2G23800.1; AT2G23800.1; AT2G23800.
DR KEGG; ath:AT2G23800; -.
DR Araport; AT2G23800; -.
DR TAIR; locus:2048993; AT2G23800.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; O04046; -.
DR OMA; FEFDPYM; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; O04046; -.
DR BioCyc; ARA:AT2G23800-MON; -.
DR BioCyc; MetaCyc:AT2G23800-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:O04046; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04046; baseline and differential.
DR Genevisible; O04046; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
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: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 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; Endoplasmic reticulum; Isoprene biosynthesis;
KW Magnesium; Metal-binding; Reference proteome; Signal; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..376
FT /note="Heterodimeric geranylgeranyl pyrophosphate synthase
FT large subunit 2"
FT /id="PRO_0000045402"
FT BINDING 125
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 128
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 157
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 175
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 261
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT CONFLICT 146..147
FT /note="AM -> TI (in Ref. 1; AAB67730)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="H -> D (in Ref. 1; AAB67730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41339 MW; 1B643EC4086BD43B CRC64;
MEPQILFLYL SLFILSLNFF FTNLKPRLVR LFQPSLESRV KTALLSRKEV AAFLDSPIVE
DEEGEEREEE EEGGIVSNAN FTFEFDPYMM SKAESVNKAL EEAIPVGEPL KIHEAMRYAI
LAAGKRVRPI LCLASCELVG GQENAAMPAA CAVEMIHTMS LIKDDLPCMD NDDLRRGKPT
THKVYGEGVA ILSGGALLSL AFEHMTTAEI SSERMVWAVR ELARSIGTRG LVAGQAMDIS
SEGLDLNEVG LEHLEFIHVH KTAVLLETAA VLGAIIGGGS DEEIESVRKF ARCIGLLFQV
VDDILDETKS SEELGKTAGK DQLAGKLTYP KLIGLEKSKE FVKRLTKDAR QHLQGFSSEK
VAPLVALTTF IANRNK
