ID   LALIN_LAVAN             Reviewed;         564 AA.
AC   Q2XSC5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=R-linalool synthase;
DE            Short=LaLINS;
DE            EC=4.2.3.26;
OS   Lavandula angustifolia (Lavender).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC   Lavandula.
OX   NCBI_TaxID=39329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17662687; DOI=10.1016/j.abb.2007.06.011;
RA   Landmann C., Fink B., Festner M., Dregus M., Engel K.H., Schwab W.;
RT   "Cloning and functional characterization of three terpene synthases from
RT   lavender (Lavandula angustifolia).";
RL   Arch. Biochem. Biophys. 465:417-429(2007).
CC   -!- FUNCTION: Specifically catalyzes production of (R)-(-)-linalool, the
CC       main component of lavender essential oil.
CC       {ECO:0000269|PubMed:17662687}.
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:17662687};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=42.7 uM for geranyl diphosphate {ECO:0000269|PubMed:17662687};
CC         Note=kcat is 0.039 sec(-1) with geranyl diphosphate as substrate.;
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:17662687};
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ263741; ABB73045.1; -; mRNA.
DR   AlphaFoldDB; Q2XSC5; -.
DR   SMR; Q2XSC5; -.
DR   PRIDE; Q2XSC5; -.
DR   BioCyc; MetaCyc:MON-13458; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0034008; F:R-linalool synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0046246; P:terpene biosynthetic process; IEA:UniProt.
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   Lyase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..564
FT                   /note="R-linalool synthase"
FT                   /id="PRO_0000418950"
FT   MOTIF           320..324
FT                   /note="DDXXD motif"
FT   BINDING         320
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         468
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   564 AA;  65654 MW;  19E23FD94DFA1E5B CRC64;
     MSININMPAA AVLRPFRCSQ LHVDETRRSG NYRPSAWDSN YIQSLNSQYK EKKCLTRLEG
     LIEQVKELKG TKMEAVQQLE LIDDSQNLGL SYYFQDKIKH ILNLIYNDHK YFYDSEAEGM
     DLYFTALGFR LFRQHGFKVS QEVFDRFKNE NGTYFKHDDT KGLLQLYEAS FLVREGEETL
     EQAREFATKS LQRKLDEDGD GIDANIESWI RHSLEIPLHW RAQRLEARWF LDAYARRPDM
     NPVIFELAKL NFNIVQATQQ EELKALSRWW SSLGLAEKLP FVRDRLVESY FWAIPLFEPH
     QYGYQRKVAT KIITLITSLD DVYDIYGTLD ELQLFTNLFE RWDNASIGRL PEYLQLFYFA
     IHNFVSEVAY DILKEKGFTS IVYLQRSWVD LLKGYLKEAK WYNSGYTPSL EEYFDNAFMT
     IGAPPVLSQA YFTLGSSMEK PIIESMYEYD NILRVSGMLV RLPDDLGTSS FEMERGDVPK
     SVQLYMKETN ATEEEAVEHV RFLNREAWKK MNTAEAAGDS PLVSDVVAVA ANLGRAAQFM
     YFDGDGNQSS LQQWIVSMLF EPYA