(data stored in ACNUC13479 zone)

SWISSPROT: 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   07-JUN-2017, entry version 106.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthase 4;
DE            Short=GGPP synthase 4;
DE            Short=GGPS4;
DE            EC=2.5.1.-;
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase 4;
DE   AltName: Full=Dimethylallyltranstransferase 4;
DE            EC=2.5.1.1;
DE   AltName: Full=Farnesyl diphosphate synthase 4;
DE   AltName: Full=Farnesyltranstransferase 4;
DE            EC=2.5.1.29;
DE   AltName: Full=Geranyltranstransferase 4;
DE            EC=2.5.1.10;
DE   Flags: Precursor;
GN   Name=GGPP4; OrderedLocusNames=At2g18640; ORFNames=F24H14.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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   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
RT   organs are localized into three subcellular compartments in
RT   Arabidopsis.";
RL   Plant Physiol. 122:1045-1056(2000).
CC   -!- FUNCTION: Catalyzes the trans-addition of the three molecules of
CC       IPP onto DMAPP to form geranylgeranyl pyrophosphate.
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC       = diphosphate + (2E,6E)-farnesyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranylgeranyl diphosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
CC       biosynthesis; farnesyl diphosphate from geranyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
CC       biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
CC       and isopentenyl diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC       biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate
CC       and isopentenyl diphosphate: step 1/1.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:10759500}.
CC   -!- TISSUE SPECIFICITY: Faintly expressed in flowers.
CC       {ECO:0000269|PubMed:10759500}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC       {ECO:0000305}.
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   UniGene; At.66219; -.
DR   ProteinModelPortal; Q9SLG2; -.
DR   SMR; Q9SLG2; -.
DR   BioGrid; 1736; 3.
DR   MINT; MINT-8059623; -.
DR   STRING; 3702.AT2G18640.1; -.
DR   PaxDb; Q9SLG2; -.
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   eggNOG; COG0142; LUCA.
DR   InParanoid; Q9SLG2; -.
DR   KO; K13789; -.
DR   OMA; DFKPYMI; -.
DR   OrthoDB; EOG09360HVD; -.
DR   PhylomeDB; Q9SLG2; -.
DR   BioCyc; ARA:AT2G18640-MONOMER; -.
DR   BioCyc; MetaCyc:AT2G18640-MONOMER; -.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   UniPathway; UPA00389; UER00564.
DR   PRO; PR:Q9SLG2; -.
DR   Proteomes; UP000006548; Chromosome 2.
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: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   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom.
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   2: Evidence at transcript level;
DR   PRODOM; Q9SLG2.
DR   SWISS-2DPAGE; Q9SLG2.
KW   Carotenoid biosynthesis; Complete proteome; Endoplasmic reticulum;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Signal; Transferase.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    372       Geranylgeranyl pyrophosphate synthase 4.
FT                                /FTId=PRO_0000045404.
FT   METAL       160    160       Magnesium 1. {ECO:0000250}.
FT   METAL       160    160       Magnesium 2. {ECO:0000250}.
FT   METAL       166    166       Magnesium 1. {ECO:0000250}.
FT   METAL       166    166       Magnesium 2. {ECO:0000250}.
FT   METAL       298    298       Magnesium 3. {ECO:0000250}.
FT   BINDING     121    121       Isopentenyl diphosphate. {ECO:0000250}.
FT   BINDING     124    124       Isopentenyl diphosphate. {ECO:0000250}.
FT   BINDING     153    153       Isopentenyl diphosphate. {ECO:0000250}.
FT   BINDING     171    171       Dimethylallyl diphosphate. {ECO:0000250}.
FT   BINDING     172    172       Isopentenyl diphosphate. {ECO:0000250}.
FT   BINDING     257    257       Dimethylallyl diphosphate. {ECO:0000250}.
FT   BINDING     258    258       Dimethylallyl diphosphate. {ECO:0000250}.
FT   BINDING     295    295       Dimethylallyl diphosphate. {ECO:0000250}.
FT   BINDING     312    312       Dimethylallyl diphosphate. {ECO:0000250}.
FT   BINDING     322    322       Dimethylallyl diphosphate. {ECO:0000250}.
FT   CONFLICT    152    152       I -> M (in Ref. 4; AAA96328).
FT                                {ECO:0000305}.
FT   CONFLICT    303    303       E -> V (in Ref. 4; AAA96328).
FT                                {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
//

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