GGPP4_ARATH
ID GGPP4_ARATH Reviewed; 372 AA.
AC Q9SLG2; Q1PF45; Q39107;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase 4 {ECO:0000303|PubMed:10759500};
DE Short=GGPP synthase 4 {ECO:0000303|PubMed:10759500};
DE Short=GGPS4 {ECO:0000303|PubMed:10759500};
DE EC=2.5.1.- {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 4 {ECO:0000305};
DE EC=2.5.1.10 {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
DE AltName: Full=Dimethylallyltranstransferase 4 {ECO:0000305};
DE EC=2.5.1.1 {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
DE AltName: Full=Farnesyl diphosphate synthase 4 {ECO:0000305};
DE AltName: Full=Farnesyltranstransferase 4 {ECO:0000305};
DE AltName: Full=Geranylgeranyl diphosphate synthase 4 {ECO:0000305};
DE EC=2.5.1.29 {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
DE AltName: Full=Geranyltranstransferase 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=GGPP4 {ECO:0000303|PubMed:10759500};
GN Synonyms=GGPS3 {ECO:0000303|PubMed:23729351};
GN OrderedLocusNames=At2g18640 {ECO:0000312|Araport:AT2G18640};
GN ORFNames=F24H14.2 {ECO:0000312|EMBL:AAM15136.1};
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=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 [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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-304.
RC STRAIN=cv. Wassilewskija;
RA Bartley G.E., Scolnik P.A., Giuliano G.;
RT "Molecular biology of carotenoid biosynthesis in plants.";
RL Plant Physiol. 45:287-301(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23729351; DOI=10.1007/s11103-013-0070-z;
RA Beck G., Coman D., Herren E., Ruiz-Sola M.A., Rodriguez-Concepcion M.,
RA Gruissem W., Vranova E.;
RT "Characterization of the GGPP synthase gene family in Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 82:393-416(2013).
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of
CC isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to
CC form geranylgeranyl diphosphate. {ECO:0000269|PubMed:10759500,
CC ECO:0000269|PubMed:23729351}.
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 Evidence={ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC Evidence={ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
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 Evidence={ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
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 Evidence={ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:10759500};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P14324};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351}.
CC -!- TISSUE SPECIFICITY: Faintly expressed in flowers (PubMed:10759500).
CC Expressed in roots and siliques (PubMed:23729351).
CC {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:23729351}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AC005724; AAD08933.1; -; Genomic_DNA.
DR EMBL; AC006135; AAM15136.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06788.1; -; Genomic_DNA.
DR EMBL; DQ446521; ABE65826.1; -; mRNA.
DR EMBL; L22347; AAA96328.1; -; Genomic_DNA.
DR PIR; G84566; G84566.
DR RefSeq; NP_179454.1; NM_127420.2.
DR AlphaFoldDB; Q9SLG2; -.
DR SMR; Q9SLG2; -.
DR BioGRID; 1736; 3.
DR STRING; 3702.AT2G18640.1; -.
DR PaxDb; Q9SLG2; -.
DR PRIDE; Q9SLG2; -.
DR ProteomicsDB; 221842; -.
DR EnsemblPlants; AT2G18640.1; AT2G18640.1; AT2G18640.
DR GeneID; 816379; -.
DR Gramene; AT2G18640.1; AT2G18640.1; AT2G18640.
DR KEGG; ath:AT2G18640; -.
DR Araport; AT2G18640; -.
DR TAIR; locus:2046258; AT2G18640.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; Q9SLG2; -.
DR OMA; SARMCGY; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; Q9SLG2; -.
DR BioCyc; ARA:AT2G18640-MON; -.
DR BioCyc; MetaCyc:AT2G18640-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:Q9SLG2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLG2; baseline and differential.
DR Genevisible; Q9SLG2; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..372
FT /note="Geranylgeranyl pyrophosphate synthase 4"
FT /id="PRO_0000045404"
FT BINDING 121
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 124
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 153
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 171
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 257
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT CONFLICT 152
FT /note="I -> M (in Ref. 4; AAA96328)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> V (in Ref. 4; AAA96328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40936 MW; C16F7F798BB7051A CRC64;
MEAQNIFLYL LIVFLSLHFV FTTLKGRLSP ANTRRLIRLL HIPIKSPVAA AIFARKDTRE
FLDSSIKLVN EEDDFGFSFD FKPYMISKAE TINRALDEAI PLIEPLNIHK AMRYAILAGG
KRVRPILCLA ACELVGGEER LAIQAACAVE MIHTMSLIKD DLPCMDNDDL RRGKPTTHKV
FGESVAILSG GALLALAFEH LTEADVSSKK MVRAVKELAK SIGTKGLVAG QAKDLSSEGL
EQNDVGLEDL EYIHVHKTGS LLEASAVIGA VIGGGTEKEI EKVRNFARCI GLLFQVVDDI
LDETKSSEEL GKTAGKDKVA GKLTYPKVIG VEKSKEFVEK LKRDAREHLQ GFDSDKVKPL
IALTNFIANR NH
