LLOS_MENAQ
ID LLOS_MENAQ Reviewed; 606 AA.
AC Q8H2B4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=R-linalool synthase, chloroplastic;
DE EC=4.2.3.26;
DE Flags: Precursor;
OS Mentha aquatica (Water mint).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC Mentha.
OX NCBI_TaxID=190902;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RX PubMed=12176064; DOI=10.1016/s0003-9861(02)00348-x;
RA Crowell A.L., Williams D.C., Davis E.M., Wildung M.R., Croteau R.;
RT "Molecular cloning and characterization of a new linalool synthase.";
RL Arch. Biochem. Biophys. 405:112-121(2002).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of (3R)-
CC linalool from geranyl diphosphate, but not from farnesyl diphosphate or
CC geranylgeranyl 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:12176064};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:12176064};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:12176064};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000305|PubMed:12176064};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for Geranyl diphosphate {ECO:0000269|PubMed:12176064};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:12176064};
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; AY083653; AAL99381.1; -; mRNA.
DR AlphaFoldDB; Q8H2B4; -.
DR SMR; Q8H2B4; -.
DR KEGG; ag:AAL99381; -.
DR BioCyc; MetaCyc:MON-12781; -.
DR BRENDA; 4.2.3.26; 8510.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
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:0033383; P:geranyl diphosphate metabolic 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; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..606
FT /note="R-linalool synthase, chloroplastic"
FT /id="PRO_0000398173"
FT MOTIF 363..367
FT /note="DDXXD motif"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 606 AA; 70535 MW; 73BF6C39EB534E0C CRC64;
MCTIISVNHH HVAILSKPKV KLFHTKNKRS ASINLPWSLS PSSSAASRPI SCSISSKLYT
ISSAQEETRR SGNYHPSVWD FDFIQSLDTD HYKEEKQLER EEELIMEVKK LLGAKMEATK
QLELIDDLQN LGLSYFFRDE IKNILNSIYK IFQNNNSTKV GDLHFTSLGF RLLRQHGFNV
SQGVFDCFKN EHGSDFEKTL IGEDTKGVLQ LYEASFLLRE GEDTLEVARK FSTEFLEEKL
KAGIDGDNLS SSIGHSLEIP LHWRIQRLEE RWFLDAYSRR KDMNPIIFEL AKLDFNIIQA
TQQEELKDLS RWWNDSSLPQ KLPFVRDRLV ESYYWALGLF EAHKFGYERK TAAKIITLIT
ALDDVYDIYG TLDELQLFTH VIRRWDTESA TQLPYYLQLF YFVLYNFVSE VAYHILKEEG
FISIPFLHRA WVDLVEGYLQ EAKWYYTKYT PTMEEYLNYA SITIGAPAVI SQIYFMLAKS
KEKPVIESFY EYDEIIRLSG MLVRLPDDLG TLPFEMKRGD VAKSIQIYMK EQNATREEAE
EHVRFMIREA WKEMNTTMAA NSDLRGDVVM AAANLGRDAQ FMYLDGDGNH SQLQHRIANL
LFKPYV
