ID   LIS_CLABR               Reviewed;         870 AA.
AC   Q96376;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=S-linalool synthase;
DE            EC=4.2.3.25;
GN   Name=LIS;
OS   Clarkia breweri (Fairy fans) (Eucharidium breweri).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX   NCBI_TaxID=36903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=8768373; DOI=10.2307/3870357;
RA   Dudareva N., Cseke L., Blanc V.M., Pichersky E.;
RT   "Evolution of floral scent in Clarkia: novel patterns of S-linalool
RT   synthase gene expression in the C. breweri flower.";
RL   Plant Cell 8:1137-1148(1996).
CC   -!- FUNCTION: Involved in the biosynthesis of the acyclic monoterpene S-
CC       linalool, a major component of the strong sweet scent of the C.breweri
CC       flowers. {ECO:0000269|PubMed:8768373}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate;
CC         Xref=Rhea:RHEA:24116, ChEBI:CHEBI:98, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.25;
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   -!- TISSUE SPECIFICITY: Highly expressed in cells of the transmitting tract
CC       of the stigma and style and in the epidermal cells of petals, as well
CC       as in stamens. {ECO:0000269|PubMed:8768373}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; U58314; AAC49395.1; -; mRNA.
DR   AlphaFoldDB; Q96376; -.
DR   SMR; Q96376; -.
DR   KEGG; ag:AAC49395; -.
DR   BioCyc; MetaCyc:MON-13464; -.
DR   BRENDA; 4.2.3.25; 1437.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0034007; F:S-linalool synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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   SUPFAM; SSF48239; SSF48239; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..870
FT                   /note="S-linalool synthase"
FT                   /id="PRO_0000263074"
FT   MOTIF           547..551
FT                   /note="DDXXD motif"
FT   BINDING         547
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         547
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         551
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         551
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         689
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         693
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         697
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   870 AA;  99790 MW;  B33BDFD22A438E39 CRC64;
     MQLITNFSSS SSELQFLVDK VKRESLSSSS SNTQNLFLST SPYDTAWLAL IPHPHHHHHH
     GRPMFEKCLQ WILHNQTPQG FWAAAGDNIS DTDDDVTLDC LLSTLACLVA LKRWQLAPDM
     IHKGLEFVNR NTERLVMKQK PSDVPRWFTI MFPAMLELAG ASSLRVDFSE NLNRILVELS
     QNRDDILTRE EVDEKKQYSP LLLFLEALPA QSYDNDVLKQ IIDKNLSNDG SLLQSPSATA
     RAYMITGNTR CLSYLHSLTN SCSNGGVPSF YPVDDDLHDL VMVNQLTRSG LTEHLIPEID
     HLLLKVQKNY KYKKASPKSL YSIAAELYRD SLAFWLLRVN NHWVSPSIFC WFLDDDEIRD
     HIETNYEEFA AVLLNVYRAT DLMFSGEVQL VEARSFATKN LEKILATGNI HKTNADISSS
     LHKMIEHELR VPWTARMDHV ENRIWIEEIA SSALWFGKSS YLRLSCFHKM SLQQLAVKNY
     TLRQLVYRDE LAEVERWSKE RGLCDMGFCR EKTGYCYYAF AASTCLPWSS DVRLVLTKAA
     VVITVADDFF DVEGSMVDLE KLTDAVRRWD AEGLGSHSKT IFEALDDLVN EVRLKCFQQN
     GQDIKNNLQQ LWYETFHSWL MEAKWGKGLT SKPSVDVYLG NAMTSIAAHT MVLTASCLLG
     PGFPVHQLWS QRRHQDITSL LMVLTRLLND IQSYLKEEDE GKINYVWMYM IENNQASIDD
     SVRHVQTIIN VKKQEFIQRV LSDQHCNLPK SFKQLHFSCL KVFNMFFNSS NIFDTDTDLL
     LDIHEAFVSP PQVPKFKPHI KPPHQLPATL QPPHQPQQIM VNKKKVEMVY KSYHHPFKVF
     TLQKKQSSGH GTMNPRASIL AGPNIKLCFS