GGPP3_ARATH
ID GGPP3_ARATH Reviewed; 360 AA.
AC Q9LUD9; F4IW70; Q38918; Q8GY09; Q8LBX9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase 3, chloroplastic;
DE Short=GGPP synthase 3;
DE Short=GGPS3;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 3;
DE AltName: Full=Dimethylallyltranstransferase 3;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 3;
DE AltName: Full=Farnesyltranstransferase 3;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase 3;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN Name=GGPP3; OrderedLocusNames=At3g14550; ORFNames=MIE1.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-360.
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 [6]
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).
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP
CC onto DMAPP to form geranylgeranyl pyrophosphate.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10759500}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots.
CC {ECO:0000269|PubMed:10759500}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB023038; BAB02387.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75537.1; -; Genomic_DNA.
DR EMBL; AK117933; BAC42571.1; -; mRNA.
DR EMBL; AY086932; AAM64496.1; -; mRNA.
DR EMBL; U44877; AAB67731.1; -; mRNA.
DR PIR; S71231; S71231.
DR RefSeq; NP_001319550.1; NM_001338122.1.
DR RefSeq; NP_001326728.1; NM_001338123.1.
DR RefSeq; NP_188073.2; NM_112315.4.
DR PDB; 5E8H; X-ray; 2.30 A; A/B=40-360.
DR PDBsum; 5E8H; -.
DR AlphaFoldDB; Q9LUD9; -.
DR SMR; Q9LUD9; -.
DR STRING; 3702.AT3G14550.1; -.
DR PaxDb; Q9LUD9; -.
DR PRIDE; Q9LUD9; -.
DR GeneID; 820681; -.
DR KEGG; ath:AT3G14550; -.
DR Araport; AT3G14550; -.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; Q9LUD9; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q9LUD9; -.
DR BioCyc; MetaCyc:AT3G14550-MON; -.
DR BRENDA; 2.5.1.81; 399.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:Q9LUD9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUD9; baseline and differential.
DR Genevisible; Q9LUD9; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IBA:GO_Central.
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 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; Carotenoid biosynthesis; Chloroplast; Isoprene biosynthesis;
KW Magnesium; Metal-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..360
FT /note="Geranylgeranyl pyrophosphate synthase 3,
FT chloroplastic"
FT /id="PRO_0000045403"
FT REGION 24..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 109
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 138
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 156
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 245
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="S -> N (in Ref. 3; BAC42571)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="G -> R (in Ref. 4; AAM64496)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="V -> F (in Ref. 2; AEE75537)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> T (in Ref. 3; BAC42571)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> P (in Ref. 4; AAM64496)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="K -> E (in Ref. 4; AAM64496)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="Y -> H (in Ref. 5; AAB67731)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="C -> F (in Ref. 5; AAB67731)"
FT /evidence="ECO:0000305"
FT HELIX 60..84
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 124..146
FT /evidence="ECO:0007829|PDB:5E8H"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5E8H"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 168..190
FT /evidence="ECO:0007829|PDB:5E8H"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 265..293
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 319..335
FT /evidence="ECO:0007829|PDB:5E8H"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:5E8H"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:5E8H"
SQ SEQUENCE 360 AA; 38844 MW; FDB5244FCBBB2742 CRC64;
MATTVHLSSF SLFIQSRGRR DNSISSVKSL KKRTGLSPSS ALTSQGGRDM IPPEGKCNDH
NSAFDFKLYM IRKAESVNAA LDVSVPLREP LTVQEAVRYS LLAGGKRVRP LLCIAVCELV
GGDEATAMSA ACAVEMIHTS SLIHDDLPCM DNADLRRGKP TNHKVYGEDM AVLAGDALLA
LAFEHMTVVS SGLVAPERMI RAVVELARAI GTTGLVAGQM IDLASERLNP DKVGLEHLEF
IHLHKTAALL EAAAVLGVIM GGGTEEEIEK LRKYARCIGL LFQVVDDILD VTKSTEELGK
TAGKDVMAGK LTYPRLIGLE RSKEVAEKLR REAEEQLLGF DPSKAAPLVA LASYIACRHN
