GFDPS_LEUCN
ID GFDPS_LEUCN Reviewed; 364 AA.
AC A0A0U3BRC5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Geranylfarnesyl diphosphate synthase, chloroplastic {ECO:0000303|PubMed:26941091};
DE Short=LcGFDPS {ECO:0000303|PubMed:26941091};
DE EC=2.5.1.81 {ECO:0000269|PubMed:26941091};
DE Flags: Precursor;
GN Name=GFDPS {ECO:0000303|PubMed:26941091};
GN Synonyms=IDS3 {ECO:0000303|PubMed:26941091};
OS Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Pogostemoneae;
OC Leucosceptrum.
OX NCBI_TaxID=694369;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION
RP BY JASMONIC ACID AND SALICYLIC ACID.
RX PubMed=26941091; DOI=10.1105/tpc.15.00715;
RA Liu Y., Luo S.-H., Schmidt A., Wang G.-D., Sun G.-L., Grant M., Kuang C.,
RA Yang M.-J., Jing S.-X., Li C.-H., Schneider B., Gershenzon J., Li S.-H.;
RT "A geranylfarnesyl diphosphate synthase provides the precursor for
RT sesterterpenoid (C25) formation in the glandular trichomes of the mint
RT species Leucosceptrum canum.";
RL Plant Cell 28:804-822(2016).
RN [2]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of leucosceptrane
CC sesterterpenoids natural products, which are playing defensive roles
CC toward herbivorus insects (e.g. Spodoptera exigua) (PubMed:26941091).
CC Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the
CC allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFDP), the
CC C(25) prenyl diphosphate precursor to all sesterterpenoids
CC (PubMed:26941091). Geranylgeranyl diphosphate (GGPP) is the preferred
CC substrate, however dimethylallyl diphosphate (DMADP), farnesyl
CC diphosphate (FDP) and geranyl diphosphate (GDP) can also be used as
CC allylic substrate (PubMed:26941091). {ECO:0000269|PubMed:26941091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81; Evidence={ECO:0000269|PubMed:26941091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25695;
CC Evidence={ECO:0000269|PubMed:26941091};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + 2 isopentenyl diphosphate =
CC (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 2 diphosphate;
CC Xref=Rhea:RHEA:66852, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:26941091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66853;
CC Evidence={ECO:0000269|PubMed:26941091};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 3 isopentenyl diphosphate =
CC (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 3 diphosphate;
CC Xref=Rhea:RHEA:66856, ChEBI:CHEBI:33019, ChEBI:CHEBI:57907,
CC ChEBI:CHEBI:58057, ChEBI:CHEBI:128769;
CC Evidence={ECO:0000269|PubMed:26941091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66857;
CC Evidence={ECO:0000269|PubMed:26941091};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + 4 isopentenyl diphosphate =
CC (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate;
CC Xref=Rhea:RHEA:66860, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:128769;
CC Evidence={ECO:0000269|PubMed:26941091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66861;
CC Evidence={ECO:0000269|PubMed:26941091};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34.89 uM for dimethylallyl diphosphate (in the presence of
CC isopentenyl diphosphate) {ECO:0000269|PubMed:26941091};
CC KM=3.04 uM for isopentenyl diphosphate (in the presence of
CC geranylgeranyl diphosphate) {ECO:0000269|PubMed:26941091};
CC KM=6.28 uM for geranyl diphosphate (in the presence of isopentenyl
CC diphosphate) {ECO:0000269|PubMed:26941091};
CC KM=4.10 uM for farnesyl diphosphate (in the presence of isopentenyl
CC diphosphate) {ECO:0000269|PubMed:26941091};
CC KM=1.65 uM for geranylgeranyl diphosphate (in the presence of
CC isopentenyl diphosphate) {ECO:0000269|PubMed:26941091};
CC Note=kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as
CC substrate (in the presence of isopentenyl diphosphate)
CC (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl
CC diphosphate as substrate (in the presence of geranylgeranyl
CC diphosphate) (PubMed:26941091). kcat is 6.16x10(-6) sec(-1) with
CC geranyl diphosphate as substrate (in the presence of isopentenyl
CC diphosphate) (PubMed:26941091). kcat is 7.19x10(-6) sec(-1) with
CC farnesyl diphosphate as substrate (in the presence of isopentenyl
CC diphosphate) (PubMed:26941091). kcat is 5.17x10(-6) sec(-1) with
CC geranylgeranyl diphosphate as substrate (in the presence of
CC isopentenyl diphosphate) (PubMed:26941091).
CC {ECO:0000269|PubMed:26941091};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30468448}.
CC -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:26941091}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P34802}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:26941091}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in glandular trichomes, and, at
CC low levels, in leaves, stems and flowers.
CC {ECO:0000269|PubMed:26941091}.
CC -!- INDUCTION: Induced by jasmonic acid, thus triggering sesterterpenoids
CC accumulation and reducing feeding and growth of the herbivorus insect
CC Spodoptera exigua (PubMed:26941091). Accumulates transiently after
CC salicylic acid treatment (PubMed:26941091).
CC {ECO:0000269|PubMed:26941091}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; KT312959; ALT16903.1; -; mRNA.
DR AlphaFoldDB; A0A0U3BRC5; -.
DR SMR; A0A0U3BRC5; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IDA:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IDA:UniProtKB.
DR GO; GO:0009625; P:response to insect; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding; Plastid;
KW Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..364
FT /note="Geranylfarnesyl diphosphate synthase, chloroplastic"
FT /id="PRO_0000452691"
FT BINDING 72
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 111
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 143
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 161
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 162
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 249
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 250
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 287
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 294
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 304
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 314
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 364 AA; 39476 MW; E4929C92D224C5C4 CRC64;
MSHCTIFLYK YFPGKPRYQH CSFLHPLNHK LKSLFLPITG SRFLSNSTFS VSDSAHSHQA
KPHVRNAQFD FKAYMLEKIT AVNQALDAAL PVREPVKIHE AMRYSLLLGG KRICPIVCLA
ACHLVGGDES TAMPSAAALE MIHAMSLMHD DLPCMDNDDL RRGRPSNHVV FGEGATVLAG
YALIARAFEH IATATQGVGP GKILRVIGEL AQLIGAEGVV GGQVVDLRCG GEGQMAIGLE
QLEYIHLHKT AASVEASAVA GAVLGGASEE EIERLRKYSR SAGLLFQVVD DILDVTKSSE
ELGKTAGKDL AAGKTTYPKL LGMEKSREMA EKLKREAQEQ LLGFDPIKAA PLIALVDFIA
YRDK
