LLOS_OCIBA
ID LLOS_OCIBA Reviewed; 574 AA.
AC Q5SBP3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=R-linalool synthase, chloroplastic;
DE EC=4.2.3.26;
DE Flags: Precursor;
GN Name=LIS;
OS Ocimum basilicum (Sweet basil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC Ocimum.
OX NCBI_TaxID=39350;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Peltate glandular trichome;
RX PubMed=15516500; DOI=10.1104/pp.104.051318;
RA Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E.,
RA Lewinsohn E., Pichersky E.;
RT "The biochemical and molecular basis for the divergent patterns in the
RT biosynthesis of terpenes and phenylpropenes in the peltate glands of three
RT cultivars of basil.";
RL Plant Physiol. 136:3724-3736(2004).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of (3R)-
CC linalool from geranyl diphosphate.
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:15516500};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AY693647; AAV63789.1; -; mRNA.
DR AlphaFoldDB; Q5SBP3; -.
DR SMR; Q5SBP3; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 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; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..574
FT /note="R-linalool synthase, chloroplastic"
FT /id="PRO_0000398174"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 324..328
FT /note="DDXXD motif"
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 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 65822 MW; E8AB2156957B85FD CRC64;
MSCARITVTL PYRSAKTSIQ RGITHCPALL RPRFSACTPL ASAVPLSSTP LINGDNSPLK
NTHQHVEERS SKRREYLLEE TARKLQRNDT ESVEKLKLID NIQRLGIGYY FEDAIDAVLR
SPFSAEEEED LFTAALRFRL LRHNGIQVTP EIFLKFKDER GEFDESDTLG LLSLYEASNL
GVTGEEILEE AMEFAEPRLR RSLSELAAPL RSEVAQALDV PRHLRMARLE ARRFIEQYGK
QSDHDGDLLE LAILDYNQVQ AQHQSELTEI TRWWKQLGLV EKLGFGRDRA LECFMWTMGI
LPHPKYSSSR IESAKAAALL YVIDDIFDTY GKMDELILFT DAIRRWDLEA MEGLPEYMKI
CYMALYNTTN EICYRVLKDT GRIALPYLKS VWIETIEAYM VEVKWFSGGS APKLEEYIEN
GASTVGAYMV LVHLFFLIGE GLTHQNVLFF KQKPYHKPFS AAGRIFRLWD DLGTSQEEEE
RGDMASSIRL FMKEYKLSTV EEARSCVLEE ISRLWKDLNE GLISIKDALP LTIVKVALNI
ARTSQVVYKH EQHTYMLSVD NYVEALFFTP LLSS
