LLOS1_ARTAN
ID LLOS1_ARTAN Reviewed; 567 AA.
AC Q9SPN0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=R-linalool synthase QH1, chloroplastic;
DE EC=4.2.3.26;
DE Flags: Precursor; Fragment;
GN Name=QH1;
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, TISSUE SPECIFICITY, AND INDUCTION
RP BY WOUNDING.
RX PubMed=10562427; DOI=10.1006/abbi.1999.1466;
RA Jia J.W., Crock J., Lu S., Croteau R., Chen X.Y.;
RT "(3R)-Linalool synthase from Artemisia annua L.: cDNA isolation,
RT characterization, and wound induction.";
RL Arch. Biochem. Biophys. 372:143-149(1999).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of (3R)-
CC linalool from geranyl diphosphate, but not from isopentenyl
CC diphosphate, dimethylallyl diphosphate, chrysanthemyl diphosphate,
CC farnesyl diphosphate, (+)-copalyl diphosphate or geranylgeranyl
CC diphosphate. {ECO:0000269|PubMed:10562427}.
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:10562427};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:10562427};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000305|PubMed:10562427};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=64 uM for geranyl diphosphate {ECO:0000269|PubMed:10562427};
CC KM=4.6 mM for magnesium {ECO:0000269|PubMed:10562427};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and lower levels in
CC inflorescences. Not detected in stems, stem epidermis, stem stele or
CC roots. {ECO:0000269|PubMed:10562427}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:10562427}.
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; AF154125; AAF13357.1; -; mRNA.
DR AlphaFoldDB; Q9SPN0; -.
DR SMR; Q9SPN0; -.
DR KEGG; ag:AAF13357; -.
DR SABIO-RK; Q9SPN0; -.
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: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 GO; GO:0009611; P:response to wounding; IEP: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; Metal-binding; Plastid; Transit peptide.
FT TRANSIT <1..24
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 25..567
FT /note="R-linalool synthase QH1, chloroplastic"
FT /id="PRO_0000398171"
FT MOTIF 319..323
FT /note="DDXXD motif"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 567 AA; 65701 MW; 49D1985524EB2B5F CRC64;
GNAYMRIYST KTTRITANAT VNAADTHVRR SANYKPSSWS FDHIQSLSSK YTGDDYVARA
NTLKDAVKTM IRKSGNSLRT LELVDELQRL GISYLFEEEI SNLLETIYYN YYKFPENWNK
INLNLKALGF RLLRQHGYHV PQEIFLNFKD KNQNLNSYLL NDVVEMLNLY EASYHSFEDE
SILDDARDIT TKYLKESLEK IDGSIFSSVT HALEQPLHWR VPRVEAKWFI ELYEKKNGMS
PTLVELAKLD FDMVQAIHLE DLKHASRWWR DTSWDTKLTF ARDLIVENFL WTIGFSYLPN
FSRGRRTITK VAVMITTLDD VYDVFGTLGE LEQFTDVINR WDIKAIEQLP DYMKICFLGL
YKSINDITHE TLANKGFLIL PYLKKAWADL CKAYLVEAQW YHRGHIPTLN EYLDNACVSI
SGPVALMHVH FLTSVSSIEE IHQCIQRTEN IVHYVSLIFR LADDLGTSLG EMERGDTLKS
IQLHMHETGA TEPEARSYIK LLINKTWKKL NKERATVNSE SSQEFIDYAT NLVRMAQFMY
GEGDEDFGLD VIKSHVLSLL FTPIQGI
