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Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2 (GGPP synthase 2) (GGPS2) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 2) (Dimethylallyltranstransferase 2) (EC 2.5.1.1) (Farnesyl diphosphate synthase 2) (Farnesyltranstransferase 2) (EC 2.5.1.29) (Geranyltranstransferase 2) (EC 2.5.1.10)

 GGPP2_ARATH             Reviewed;         376 AA.
O04046; Q38917; Q7DN59;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 2.
07-JUN-2017, entry version 116.
RecName: Full=Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2;
Short=GGPP synthase 2;
Short=GGPS2;
EC=2.5.1.-;
AltName: Full=(2E,6E)-farnesyl diphosphate synthase 2;
AltName: Full=Dimethylallyltranstransferase 2;
EC=2.5.1.1;
AltName: Full=Farnesyl diphosphate synthase 2;
AltName: Full=Farnesyltranstransferase 2;
EC=2.5.1.29;
AltName: Full=Geranyltranstransferase 2;
EC=2.5.1.10;
Flags: Precursor;
Name=GGPPS2; Synonyms=GGPP5, GGPS2; OrderedLocusNames=At2g23800;
ORFNames=F27L4.2;
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].
STRAIN=cv. Landsberg erecta; TISSUE=Flower;
Scolnik P.A., Bartley G.E.;
"Two more members of an Arabidopsis geranylgeranyl pyrophosphate
synthase gene family.";
(er) Plant Gene Register PGR96-014(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-376.
PubMed=9150607; DOI=10.1093/oxfordjournals.pcp.a029174;
Zhu X.F., Suzuki K., Okada K., Tanaka K., Nakagawa T., Kawamukai M.,
Matsuda K.;
"Cloning and functional expression of a novel geranylgeranyl
pyrophosphate synthase gene from Arabidopsis thaliana in Escherichia
coli.";
Plant Cell Physiol. 38:357-361(1997).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-376, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
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).
[9]
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).
-!- 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 is not changed. {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 (By similarity). Part of a heterodimeric
geranyl(geranyl)diphosphate synthase. Interacts with GGR.
{ECO:0000250, ECO:0000269|PubMed:19482937}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:10759500}.
-!- TISSUE SPECIFICITY: Mainly expressed in flowers.
{ECO:0000269|PubMed:10759500}.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB67730.1; Type=Frameshift; Positions=5; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U44876; AAB67730.1; ALT_FRAME; mRNA.
EMBL; AC004482; AAC17083.1; -; Genomic_DNA.
EMBL; CP002685; AEC07492.1; -; Genomic_DNA.
EMBL; BT005328; AAO63392.1; -; mRNA.
EMBL; AK117954; BAC42592.1; -; mRNA.
EMBL; AY087521; AAM65063.1; -; mRNA.
EMBL; D85029; BAA19583.1; -; mRNA.
PIR; S71230; S71230.
PIR; T02429; T02429.
RefSeq; NP_179960.1; NM_127943.3.
UniGene; At.1550; -.
ProteinModelPortal; O04046; -.
SMR; O04046; -.
STRING; 3702.AT2G23800.1; -.
PaxDb; O04046; -.
PRIDE; O04046; -.
EnsemblPlants; AT2G23800.1; AT2G23800.1; AT2G23800.
GeneID; 816912; -.
Gramene; AT2G23800.1; AT2G23800.1; AT2G23800.
KEGG; ath:AT2G23800; -.
Araport; AT2G23800; -.
TAIR; locus:2048993; AT2G23800.
eggNOG; KOG0776; Eukaryota.
eggNOG; COG0142; LUCA.
HOGENOM; HOG000009101; -.
InParanoid; O04046; -.
KO; K13789; -.
OMA; CMASCEV; -.
OrthoDB; EOG09360HVD; -.
PhylomeDB; O04046; -.
BioCyc; ARA:AT2G23800-MONOMER; -.
BioCyc; MetaCyc:AT2G23800-MONOMER; -.
UniPathway; UPA00259; UER00368.
UniPathway; UPA00260; UER00369.
UniPathway; UPA00389; UER00564.
PRO; PR:O04046; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O04046; baseline and differential.
Genevisible; O04046; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
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: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.
Gene3D; 1.10.600.10; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom.
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;
Carotenoid biosynthesis; Complete proteome; Endoplasmic reticulum;
Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
Signal; Transferase.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 376 Heterodimeric geranylgeranyl
pyrophosphate synthase large subunit 2.
/FTId=PRO_0000045402.
COMPBIAS 60 72 Poly-Glu.
METAL 164 164 Magnesium 1. {ECO:0000250}.
METAL 164 164 Magnesium 2. {ECO:0000250}.
METAL 170 170 Magnesium 1. {ECO:0000250}.
METAL 170 170 Magnesium 2. {ECO:0000250}.
METAL 302 302 Magnesium 3. {ECO:0000250}.
BINDING 125 125 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 128 128 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 157 157 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 175 175 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 176 176 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 261 261 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 262 262 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 299 299 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 316 316 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 326 326 Dimethylallyl diphosphate. {ECO:0000250}.
CONFLICT 146 147 AM -> TI (in Ref. 1; AAB67730).
{ECO:0000305}.
CONFLICT 182 182 H -> D (in Ref. 1; AAB67730).
{ECO:0000305}.
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


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