GGPP8_ARATH
ID GGPP8_ARATH Reviewed; 361 AA.
AC Q9LRR0; F4IW66;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative geranylgeranyl pyrophosphate synthase 8, chloroplastic;
DE Short=GGPP synthase 8;
DE Short=GGPS8;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 8;
DE AltName: Full=Dimethylallyltranstransferase 8;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 8;
DE AltName: Full=Farnesyltranstransferase 8;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase 8;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN OrderedLocusNames=At3g14510; ORFNames=MOA2.15;
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.
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).
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: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE75533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE75533.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB01343.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB01343.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB028617; BAB01343.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75533.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_188069.1; NM_112311.2.
DR AlphaFoldDB; Q9LRR0; -.
DR SMR; Q9LRR0; -.
DR PaxDb; Q9LRR0; -.
DR PeptideAtlas; Q9LRR0; -.
DR PRIDE; Q9LRR0; -.
DR GeneID; 820674; -.
DR KEGG; ath:AT3G14510; -.
DR Araport; AT3G14510; -.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; Q9LRR0; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q9LRR0; -.
DR BioCyc; ARA:AT3G14510-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LRR0; baseline and differential.
DR Genevisible; Q9LRR0; 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 5: Uncertain;
KW Carotenoid biosynthesis; Chloroplast; Isoprene biosynthesis; Magnesium;
KW Metal-binding; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..361
FT /note="Putative geranylgeranyl pyrophosphate synthase 8,
FT chloroplastic"
FT /id="PRO_0000402122"
FT REGION 24..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 110
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 139
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 157
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 246
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 247
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 301
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
SQ SEQUENCE 361 AA; 38896 MW; 2116D81A015EA89F CRC64;
MATTVHLSSF SLFIQSRGRR DNSISSVKSL KKRTGLSPSS ALTSQGGRDM IPPQGKSNDH
NSAFDFKLYM IRKAESVNAA LDVSIVPLRE PLTVQEAVRY SLLAGGKRVR PLLCIAVCEL
VGGDEATAMS AACAVEMIHT SSLIHDDLPC MDNADLRRGK PTNHKVFGED MAVLAGDALL
ALAFEHMTVV SSGLVASERM IRAVVELARA IGTKGLVAGQ VVDLSSERLN PHDVGLERLE
FIHLHKTAAL LEAAAVIGAI MGGGTEEEIE KLRKYARCIG LLFQVVDDIL DVTKSTEELG
KTAGKDVMAG KLTYPRLIGL ERSREVAEKL SREAEEQLLG FESDKAAPLV ALASYISCRN
D
