LIMNS_PICSI
ID LIMNS_PICSI Reviewed; 634 AA.
AC Q20HU7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=(-)-limonene synthase, chloroplastic {ECO:0000303|PubMed:16415217};
DE Short=PsTPS-Lim {ECO:0000303|PubMed:16415217};
DE EC=4.2.3.16 {ECO:0000269|PubMed:16415217};
DE Flags: Precursor;
GN Name=TPS-Lim {ECO:0000303|PubMed:16415217};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP INDUCTION BY WOUNDING.
RX PubMed=16415217; DOI=10.1104/pp.105.071803;
RA Byun-McKay A., Godard K.-A., Toudefallah M., Martin D.M., Alfaro R.,
RA King J., Bohlmann J., Plant A.L.;
RT "Wound-induced terpene synthase gene expression in Sitka spruce that
RT exhibit resistance or susceptibility to attack by the white pine weevil.";
RL Plant Physiol. 140:1009-1021(2006).
CC -!- FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis
CC of monoterpene natural products (PubMed:16415217). Catalyzes the
CC conversion of (2E)-geranyl diphosphate (GPP) into (-)-limonene
CC (PubMed:16415217). Not able to use geranylgeranyl pyrophosphate (GGPP)
CC and farnesyl pyrophosphate (FPP) as substrates (PubMed:16415217).
CC {ECO:0000269|PubMed:16415217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.16;
CC Evidence={ECO:0000269|PubMed:16415217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870;
CC Evidence={ECO:0000269|PubMed:16415217};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:16415217}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:16415217}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Accumulates in apical leaders upon wounding in resistant but
CC not in susceptible to white pine weevil (Pissodes strobi) plants.
CC {ECO:0000269|PubMed:16415217}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ195275; ABA86248.1; -; mRNA.
DR OMA; QECHPNI; -.
DR BRENDA; 4.2.3.16; 8974.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0046250; P:limonene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..21
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 22..634
FT /note="(-)-limonene synthase, chloroplastic"
FT /id="PRO_0000455262"
FT MOTIF 385..389
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 634 AA; 72933 MW; 19071ADE65E38B80 CRC64;
MSPVSAIPLA YKLCLPRSLI SSSRELNPLH ITIPNLGMCR RGKSMAPASM SMILTAAVSD
DDRVQRRRGN YHSNLWDDDF IQSLSTPYGE PSYRESAERL KGEIKKMFRS MSKEDEELIT
PLNDLIQRLW MVDSVERLGI DRHFKNEIKS ALDYVYSYWN EKGIGCGRDS VVADLNSTAL
GFRTLRLHGY NVSSEVLKVF EDQNGQFACS PSKTEGEIRS ALNLYRASLI AFPGEKVMED
AEIFSSRYLK EAVQKIPDCS LSQEIAYALE YGWHTNMPRL EARNYMDVFG HPSSPWLKKN
KTQYMDGEKL LELAKLEFNI FHSLQQEELQ YISRWWKDSG LPKLAFSRHR HVEYYTLGSC
IATDPKHRAF RLGFVKTCHL NTVLDDIYDT FGTMDEIELF TEAVRRWDPS ETESLPDYMK
GVYMVLYEAL TEMAQEAEKT QGRDTLNYAR KAWEIYLDSY IQEAKWIASG YLPTFQEYFE
NGKISSAYRA AALTPILTLD VPLPEYILKG IDFPSRFNDL ASSFLRLRGD TRCYKADRAR
GEEASCISCY MKDNPGSTEE DALNHINSMI NEIIKELNWE LLRPDSNIPM PARKHAFDIT
RALHHLYKYR DGFSVATKET KSLVSRMVLE PVTL
