GGPP6_ARATH
ID GGPP6_ARATH Reviewed; 336 AA.
AC O22043; Q9XIC0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase 6, mitochondrial {ECO:0000303|PubMed:9349257};
DE Short=GGPP synthase 6 {ECO:0000303|PubMed:9349257};
DE Short=GGPS6 {ECO:0000303|PubMed:9349257};
DE EC=2.5.1.- {ECO:0000269|PubMed:9349257};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase 6;
DE AltName: Full=Dimethylallyltranstransferase 6;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase 6;
DE AltName: Full=Farnesyltranstransferase 6;
DE EC=2.5.1.29 {ECO:0000269|PubMed:9349257};
DE AltName: Full=Geranyltranstransferase 6;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN Name=GGPP6 {ECO:0000305};
GN OrderedLocusNames=At1g49530 {ECO:0000312|Araport:AT1G49530};
GN ORFNames=F13F21.3 {ECO:0000312|EMBL:AAD43148.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9349257; DOI=10.1023/a:1005898805326;
RA Zhu X., Suzuki K., Saito T., Okada K., Tanaka K., Nakagawa T., Matsuda H.,
RA Kawamukai M.;
RT "Geranylgeranyl pyrophosphate synthase encoded by the newly isolated gene
RT GGPS6 from Arabidopsis thaliana is localized in mitochondria.";
RL Plant Mol. Biol. 35:331-341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP
CC onto DMAPP to form geranylgeranyl pyrophosphate.
CC {ECO:0000269|PubMed:9349257}.
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 Evidence={ECO:0000269|PubMed:9349257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:9349257};
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.
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:0000269|PubMed:10759500,
CC ECO:0000269|PubMed:9349257}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB000835; BAA23157.1; -; Genomic_DNA.
DR EMBL; AC007504; AAD43148.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32439.1; -; Genomic_DNA.
DR EMBL; BT011230; AAR92266.1; -; mRNA.
DR EMBL; BT012158; AAS76253.1; -; mRNA.
DR RefSeq; NP_175376.1; NM_103841.3.
DR AlphaFoldDB; O22043; -.
DR SMR; O22043; -.
DR STRING; 3702.AT1G49530.1; -.
DR PaxDb; O22043; -.
DR PRIDE; O22043; -.
DR ProteomicsDB; 220745; -.
DR EnsemblPlants; AT1G49530.1; AT1G49530.1; AT1G49530.
DR GeneID; 841377; -.
DR Gramene; AT1G49530.1; AT1G49530.1; AT1G49530.
DR KEGG; ath:AT1G49530; -.
DR Araport; AT1G49530; -.
DR TAIR; locus:2010182; AT1G49530.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_0_0_1; -.
DR InParanoid; O22043; -.
DR OMA; FPERLCE; -.
DR OrthoDB; 981769at2759; -.
DR PhylomeDB; O22043; -.
DR BioCyc; MetaCyc:AT1G49530-MON; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR PRO; PR:O22043; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22043; baseline and differential.
DR Genevisible; O22043; AT.
DR GO; GO:0005739; C:mitochondrion; 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; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..336
FT /note="Geranylgeranyl pyrophosphate synthase 6,
FT mitochondrial"
FT /id="PRO_0000045405"
FT BINDING 80
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 83
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 112
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 130
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 221
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> MLCKIIIM (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="R -> C (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="I -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="K -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="F -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="P -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="R -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 36886 MW; 95F32D360003C954 CRC64;
MRPRYSLILS AMRLIRPSNR RLSSIASSDS EFISYMKNKA KSINKALDNS IPLCNNFVPL
WEPVLEVHKA MRYTLLPGGK RVRPMLCLVA CELVGGQEST AMPAACAVEM IHAASLILDD
LPCMDDDSLR RGKPTNHKVF GEKTSILASN ALRSLAVKQT LASTSLGVTS ERVLRAVQEM
ARAVGTEGLV AGQAADLAGE RMSFKNEDDE LRYLELMHVH KTAVLVEAAA VVGAIMGGGS
DEEIERLKSY ARCVGLMFQV MDDVLDETKS SEELGKTAGK DLITGKLTYP KVMGVDNARE
YAKRLNREAQ EHLQGFDSDK VVPLLSLADY IVKRQN
