LLOS2_PICSI
ID LLOS2_PICSI Reviewed; 626 AA.
AC C0PPR1; Q20HU8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=(R)-linalool synthase 2, chloroplastic {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.26 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Lin 2 {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-Lin-2 {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-Linl {ECO:0000303|PubMed:16415217};
DE Flags: Precursor;
GN Name=TPS-Lin-2 {ECO:0000303|PubMed:21385377};
GN Synonyms=TPS-Linl {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], AND 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. FB3-425; TISSUE=Green leaf;
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. FB3-425;
RX PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA Dullat H.K., Bohlmann J.;
RT "Transcriptome mining, functional characterization, and phylogeny of a
RT large terpene synthase gene family in spruce (Picea spp.).";
RL BMC Plant Biol. 11:43-43(2011).
CC -!- FUNCTION: Terpene synthase (mono-TPS) involved in the biosynthesis of
CC monoterpene natural products included in conifer oleoresin secretions
CC and volatile emissions; these compounds contribute to biotic and
CC abiotic stress defense against herbivores and pathogens
CC (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate
CC (GPP) to (R)-linalool (PubMed:21385377). {ECO:0000269|PubMed:21385377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate;
CC Xref=Rhea:RHEA:15809, ChEBI:CHEBI:28, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.26;
CC Evidence={ECO:0000269|PubMed:21385377};
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: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Accumulates in apical leaders upon wounding in both
CC resistant and susceptible to white pine weevil (Pissodes strobi)
CC plants. {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:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ195274; ABA86247.1; -; mRNA.
DR EMBL; BT070282; ACN39801.1; -; mRNA.
DR EMBL; HQ426168; ADZ45502.1; -; mRNA.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034008; F:R-linalool synthase activity; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid 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..626
FT /note="(R)-linalool synthase 2, chloroplastic"
FT /id="PRO_0000454414"
FT MOTIF 377..381
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 103
FT /note="E -> D (in Ref. 1; ABA86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="N -> K (in Ref. 1; ABA86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="D -> G (in Ref. 1; ABA86247)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="Y -> H (in Ref. 1; ABA86247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 71828 MW; 84CDA1E06D58DB58 CRC64;
MAFVSIAPLA SRCCVHKSFV SSREVKPLCR TIPTLGRCRR GKTVTPSISM CWTATVLDDG
VQRRIANHHS NLWDDSFIQS LSTPYGETSY LERADKLIGE VKEIINSISV EDGELITPLN
DLIQRLSIVD NIERLGIDRH FKNEIKSALD YVYSYWNEKG IGCGRESVIT DLNSTALGLR
TLRLHGYPVS SDVFEQFKEQ NGQFACSAIQ TEGEIKKVLN LFRASLIAFP GEKVMEEAEI
FSTIYLKEAL LKIPVCSLSR EIAYVLEYGW HMNLPRLEAR NYIDVFGQDP IYLTLNMRTQ
KLIELAKLEF NIFHSLQQEE LKHVSRWWKD SGFSQMAYAR HRHVEFYTLA SCIAIDPQHS
SFRLGFTKIT YLGTVLDDIY DTFGTMDELE LFTAAVKRWH PSAAEGLPEY MKGVYMMFYE
TVNEMAREAE KCQGRDTLNY ARQALEAYID SYMKEAKWIS SGFLPTFEEY LDNGKVSFGY
RIGTLQPILT LGIPFPHHIL QEIDFPSRLN DLAGSILRLK GDIHSYQAER SRGEESSGIS
CYMKDNPEST EEDAVTYINA MINRLLKELN WEFLKPHSNV PITSKKHAFD ILRAFYHLYK
DRDGFSVTRN EIRNLVMTTV IEHVPL
