LLOS5_ARTAN
ID LLOS5_ARTAN Reviewed; 583 AA.
AC Q9SPN1;
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 QH5, chloroplastic {ECO:0000303|PubMed:10562427};
DE EC=4.2.3.26 {ECO:0000269|PubMed:10562427};
DE Flags: Precursor;
GN Name=QH5 {ECO:0000303|PubMed:10562427};
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, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION BY
RP 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:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q84LB2};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:10562427}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in every aerial organ except for the stem
CC stele of mature plants. Not detected in roots.
CC {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 {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AF154124; AAF13356.1; -; mRNA.
DR AlphaFoldDB; Q9SPN1; -.
DR SMR; Q9SPN1; -.
DR KEGG; ag:AAF13356; -.
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; 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; Potassium;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..583
FT /note="R-linalool synthase QH5, chloroplastic"
FT /id="PRO_0000398172"
FT MOTIF 335..339
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 492
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q84LB2"
SQ SEQUENCE 583 AA; 67390 MW; A7F51589878FBFED CRC64;
MASISLFPYS ILKQTSPLAR GTAYNRIYST KTTGITVDVA ESHVRRSANY EPSSWSFDHI
QSLSSKYTGD DCVARANTLK ESVKTMIRKE GNLLRTLELV DELQRLGISY LFEGEISNLL
ETIYYNHYKF PEKWNKFDLN LKALGFRLLR QHGYHVPQEI FLNFKDKNQN LNSYLLEDVV
GMLNLYEASY HSFEDESILT EARDIATKYL KASLEKIDGS ILSLVSHALD NRLHWRVPRV
ESKWFIEVYE KRVGASPTLI ELAKLDFDMV QAIHLEDLKH ASRWWRNTSW DTKLTFARDM
LVENFLWTVG FSYLPNFSHG RRTITKVAAM ITTLDDVYDV FGTLGELEQF TDVINRWDIK
AIEQLPDYMK ICFFGLYNSI NDITYETLAT KGFLILPYIK KAWADLCKSY LVEAQWYHRG
HIPTLNEYLD NACVSISGPV ALMHVHFLTS VSSTKEIHHC IERTQNIVRY VSLIFRLTDD
LGTSLGEMER GDTLKSIQLY MHETGATEPE ARSYIKSLID KTWKKLNKER AIVSSESSRE
FIDYATNLAR MAHFMYGEGD EDFRLDVIKS HVSSLLFTPI QGI
