ID   LALIM_LAVAN             Reviewed;         602 AA.
AC   Q2XSC6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=(R)-limonene synthase;
DE            Short=LaLIMS;
DE            EC=4.2.3.20;
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: Catalyzes the formation of (R)-(+)-limonene, terpinolene,
CC       (1R,5S)-(+)-camphene, (1R,5R)-(+)-alpha-pinene, beta-myrcene and traces
CC       of alpha-phellandrene. {ECO:0000269|PubMed:17662687}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (4R)-limonene + diphosphate;
CC         Xref=Rhea:RHEA:10940, ChEBI:CHEBI:15382, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.20;
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=47.4 uM for geranyl diphosphate {ECO:0000269|PubMed:17662687};
CC         Note=kcat is 0.012 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}.
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DR   EMBL; DQ263740; ABB73044.1; -; mRNA.
DR   AlphaFoldDB; Q2XSC6; -.
DR   SMR; Q2XSC6; -.
DR   BRENDA; 4.2.3.113; 9723.
DR   BRENDA; 4.2.3.116; 9723.
DR   BRENDA; 4.2.3.121; 9723.
DR   BRENDA; 4.2.3.20; 9723.
DR   GO; GO:0034002; F:(R)-limonene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; 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..602
FT                   /note="(R)-limonene synthase"
FT                   /id="PRO_0000418951"
FT   MOTIF           356..360
FT                   /note="DDXXD motif"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         504
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         508
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   602 AA;  70345 MW;  1341E643455F34F2 CRC64;
     MSIISMHVGI LNRPAAYNHL RNLDRRASKP RHVSSTAAAT RLRVSCATQL EIKSVDETRR
     SGNYNPTAWD FNYIQSLDNQ YKKERYSTRH AELTVQVKKL LEEEMEAVQK LELIEDLKNL
     GISYPFKDNI QQILNQIYNE HKCCHNSEVE EKDLYFTALR FRLLRQQGFE VSQEVFDHFK
     NEKGTDFKPN LADDTKGLLQ LYEASFLLRE AEDTLELARQ FSTKLLQKKV DENGDDKIED
     NLLLWIRRSL ELPLHWRVQR LEARGFLDAY VRRPDMNPIV FELAKLDFNI TQATQQEELK
     DLSRWWNSTG LAEKLPFARD RVVESYFWAM GTFEPHQYGY QRELVAKIIA LATVVDDVYD
     VYGTLEELEL FTDAIRRWDR ESIDQLPYYM QLCFLTVNNF VFELAHDVLK DKSFNCLPHL
     QRSWLDLAEA YLVEAKWYHS RYTPSLEEYL NIARVSVTCP TIVSQMYFAL PIPIEKPVIE
     IMYKYHDILY LSGMLLRLPD DLGTASFELK RGDVQKAVQC YMKERNVPEN EAREHVKFLI
     REASKQINTA MATDCPFTED FAVAAANLGR VANFVYVDGD GFGVQHSKIY EQIGTLMFEP
     YP