GGPPA_ARATH
ID GGPPA_ARATH Reviewed; 344 AA.
AC Q9LJY2; A0MEX3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase 10, mitochondrial;
DE Short=GGPP synthase 10;
DE Short=GGPS10;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 10;
DE AltName: Full=Dimethylallyltranstransferase 10;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 10;
DE AltName: Full=Farnesyltranstransferase 10;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase 10;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN OrderedLocusNames=At3g20160; ORFNames=MAL21.19;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP
CC onto DMAPP to form geranylgeranyl pyrophosphate. {ECO:0000250}.
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: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28565.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP000383; BAB01876.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76342.1; -; Genomic_DNA.
DR EMBL; DQ446678; ABE65951.1; -; mRNA.
DR EMBL; DQ653096; ABK28565.1; ALT_SEQ; mRNA.
DR RefSeq; NP_188651.1; NM_112907.2.
DR PDB; 5E8K; X-ray; 3.03 A; A/B=41-344.
DR PDBsum; 5E8K; -.
DR AlphaFoldDB; Q9LJY2; -.
DR SMR; Q9LJY2; -.
DR STRING; 3702.AT3G20160.1; -.
DR PaxDb; Q9LJY2; -.
DR PRIDE; Q9LJY2; -.
DR ProteomicsDB; 224785; -.
DR EnsemblPlants; AT3G20160.1; AT3G20160.1; AT3G20160.
DR GeneID; 821560; -.
DR Gramene; AT3G20160.1; AT3G20160.1; AT3G20160.
DR KEGG; ath:AT3G20160; -.
DR Araport; AT3G20160; -.
DR TAIR; locus:2087550; AT3G20160.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; Q9LJY2; -.
DR OMA; CEGQALD; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q9LJY2; -.
DR BioCyc; ARA:AT3G20160-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:Q9LJY2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJY2; baseline and differential.
DR Genevisible; Q9LJY2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; ISS: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 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; Isoprene biosynthesis; Magnesium;
KW Metal-binding; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..344
FT /note="Geranylgeranyl pyrophosphate synthase 10,
FT mitochondrial"
FT /id="PRO_0000402124"
FT BINDING 91
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 94
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 123
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 141
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 229
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:5E8K"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 113..131
FT /evidence="ECO:0007829|PDB:5E8K"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:5E8K"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 152..172
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 182..204
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 222..245
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 249..272
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 303..319
FT /evidence="ECO:0007829|PDB:5E8K"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:5E8K"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:5E8K"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:5E8K"
SQ SEQUENCE 344 AA; 38087 MW; 4CBF9BA1207BDB39 CRC64;
MENREVFVYI VISIFRSLQF LFWRFRPRYN DVTSALTRPL TSAASYDFKF MSYMVNKAKS
VNKALEEAVP LREPELKIRE AMRYTLLSDG KRVRPMLCLA ACELVGGQES TAMSAACAIE
MLHASSLILD DLPCMDNDSL RRGKPTNHIV FGESIAILAS QALIALAVQK TTSSTFADVP
PERILKTVQE MVKAVEGLVA GQQADLAGEG MRFDSDTGLE HLEFIHIHKT AALLEAAAVM
GAIMGGGSDE EIERLRSYAR CIGLMFQVVD DVLDVTKSSE ELGKTAGKDL IAGKLTYPRL
MGVEKSKEYA ERLNIEAREH LLGFDIDKVA PLVSLADYIV NRQN
