LNOLS_PERFH
ID LNOLS_PERFH Reviewed; 603 AA.
AC C0KWV3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Linalool synthase Tps-5031L19, chloroplastic {ECO:0000303|PubMed:20447664};
DE Short=PsTps-5031L {ECO:0000303|PubMed:20447664};
DE EC=4.2.3.- {ECO:0000269|PubMed:20447664};
DE Flags: Precursor;
GN Name=Tps-5031L19 {ECO:0000303|PubMed:20447664};
OS Perilla frutescens var. hirtella (Perilla citriodora) (Perilla setoyensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX NCBI_TaxID=608512;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP COFACTOR.
RC STRAIN=cv. 5031;
RX PubMed=20447664; DOI=10.1016/j.phytochem.2010.04.006;
RA Masumoto N., Korin M., Ito M.;
RT "Geraniol and linalool synthases from wild species of perilla.";
RL Phytochemistry 71:1068-1075(2010).
CC -!- FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis
CC of monoterpenes natural products (PubMed:20447664). Catalyzes the
CC conversion of (2E)-geranyl diphosphate (GPP) into linalool
CC (PubMed:20447664). {ECO:0000269|PubMed:20447664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = diphosphate + linalool;
CC Xref=Rhea:RHEA:68708, ChEBI:CHEBI:15377, ChEBI:CHEBI:17580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC Evidence={ECO:0000269|PubMed:20447664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68709;
CC Evidence={ECO:0000269|PubMed:20447664};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20447664};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20447664};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:20447664}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; FJ644544; ACN42009.1; -; mRNA.
DR BRENDA; 4.2.3.25; 11840.
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:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0016099; P:monoterpenoid biosynthetic 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; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..603
FT /note="Linalool synthase Tps-5031L19, chloroplastic"
FT /id="PRO_0000455252"
FT MOTIF 359..363
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 603 AA; 70547 MW; DA77FA95CD0411D3 CRC64;
MSSMRTYVAI MKKPSVEHVD NVDKKASKPS WRVSLSAGLR SSCSLQLEVK PADQILTARR
SGNYQPSLWD FNYLQSLNTT HYKEVRHLKR EAELIEQVKM LLEEEMEAVQ QLELVDDLKN
LGLSYFFEDQ IKQILTFIYN EHKCFHSNSI IEAEEIRDLY FTALGFRLLR QHGFQISQEV
FDCFKNEEGS DFKARLGDDT KGLLQLYEAS FLLREGEDTL ELARQYATKF LQKKVDHELI
DDNNLLSWIL HSLEIPLHWR IQRLEARWFL DAYASRRDMN QIILELAKLD FNIIQATQQE
ELKDLSRWWK SSCLAEKLPF VRDRLVESYF WAIALFEPHQ YGYHRKIAAK IITLITSLDD
VYDIYGTLDE LQLFTDAIQR WDTESISRLP YYMQLFYMVL YNFVPRLAYD GLKEKGFITI
PYLQRSWADL VEAYLKEAKW YYNGYTPSME EYLNNAYISI GATPVISQVF FTLATSIDKP
VIDSLYEYHR ILRLSGILVR LPDDLGTSPF EMKRGDVPKA IQLYMKERNA TEIEAQEHVR
FLIREAWKEM NTATAAVDCP FTDDLVTAAA NLGRAAQFMY LDGDGNHSQL HQRIACLLFE
PYA
