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LLOS1_PICSI
ID   LLOS1_PICSI             Reviewed;         627 AA.
AC   F2XFA6;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=(R)-linalool synthase 1, chloroplastic {ECO:0000303|PubMed:21385377};
DE            EC=4.2.3.26 {ECO:0000269|PubMed:21385377};
DE   AltName: Full=Terpene synthase TPS-Lin 1 {ECO:0000303|PubMed:21385377};
DE            Short=PsTPS-Lin-1 {ECO:0000303|PubMed:21385377};
DE   Flags: Precursor;
GN   Name=TPS-Lin-1 {ECO:0000303|PubMed:21385377};
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], 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 (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   -!- 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; HQ426164; ADZ45501.1; -; 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   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..627
FT                   /note="(R)-linalool synthase 1, chloroplastic"
FT                   /id="PRO_0000454413"
FT   MOTIF           378..382
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   627 AA;  71805 MW;  D5FF9C49909486E4 CRC64;
     MAFVSIAPLA SRCCVHKSFV SSREVKPLCR TIPTLGRCRR GKTVTPSISM CWTATVLDDG
     VQRRIANHHS NLWHDSFIQS LSTPYGETSY LERADKLIGE VKEIINSISV EDGELITPLN
     DLIQRLSIVD NIERLGIDRH FKNEIKSVLD YVYSYWNEKG IGCGRESVIT DLNSTALGLR
     TLRLHGYPVS SDVLEQFKDQ NGQFACSAIQ TEGEIKSVLN LFRASLIAFP GEKVMEDAEI
     FSTIYLKEAL LTIPVCSLSR EIAYVLEHGW HTNLPRLEAR NYIDVFGQDP IYGTPNIKMT
     QKLLEIAKLE FNIFHSLQQK ELKHLSRWWK DSVFSQLTFP RHRHVEYYTL ASCIDIDPQH
     SSFRLGFAKI SHLGTVLDDI YDTFGTMDEL ELFTAALKRW HPSATKWLPE YMKGVYMMLY
     ETVNEMAREA DKSQGRDTLN YARQAWEAYI DSYMKEAKWI SSGFLPTFEE YLDNGKVSFG
     YRIGTLQPIL TLGTPFPHHI LQEIDFPSSL NRLACSILRL KGDIHTYQAE RSRGEKSSCI
     SCYMKDNPGS TEEDAVTYIN AMVNKSLKEL NWEFLRPDSN APITSKKHAF DILRAFYHLY
     KHRDGFSVAR NEIRNLVKTT VIEPVPL
 
 
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