LNOL7_PERFR
ID LNOL7_PERFR Reviewed; 604 AA.
AC C0KWV5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Linalool synthase Tps-5073L4, chloroplastic {ECO:0000303|PubMed:20447664};
DE Short=PfTps-5073L {ECO:0000303|PubMed:20447664};
DE EC=4.2.3.- {ECO:0000269|PubMed:20447664};
DE Flags: Precursor;
GN Name=Tps-5073L4 {ECO:0000303|PubMed:20447664};
OS Perilla frutescens (Beefsteak mint) (Perilla ocymoides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX NCBI_TaxID=48386;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP COFACTOR.
RC STRAIN=cv. 5073;
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; FJ644546; ACN42011.1; -; mRNA.
DR BRENDA; 4.2.3.25; 11839.
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..604
FT /note="Linalool synthase Tps-5073L4, chloroplastic"
FT /id="PRO_0000455255"
FT MOTIF 360..364
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 604 AA; 70389 MW; 5B6FAE35A32AED65 CRC64;
MSSMRIYVAI MKKPSVKHVD YVDKKASKPS WRVSSSATAG LRASSSLQLD VKKPADEILT
ARRSGNYQPS LWDFNYLQSL NTTHYKEERH LKREAELIEQ VKMLLDEEMG AVQKLDLVDD
LKNLGLSYFF EDQIKQILTF IYNEHECFRS NVEAKERDLY FTALGFRLLR QHGFQVSQEV
FDCFKNEEGS DFKASLGDDT KGLVQLYEAS FLLREGEDTL ELARQYATKF LQKKVDHELI
DDDSNLLSWI RHSLEIPLHW RIQRLEARWF LDAYATRHDV NPIILELAKL DFNIIQATQQ
EELKDLSRWW NSTCLVEKLP FVRDRLVESY FWAIALFEPH QYGYHRKIAA KIITLITSLD
DVYDIYGTLD ELQLFTDAIQ RWDTESISRL AYYMQLFYMV LYNFVSELAY DGLKEKGFIT
IPYLQRSWAD LVEAYLKEAK WFYNGYTPSM EEYLNNAYIS IGATPVISQV FFTLATSIDK
PVIESLYEYH RILRLSGMLV RLPDDLGTSP FEMKRGDVPK TIELYMKERN ATEIEAQEHV
RFLIREAWRE MNTATAAADC PFTDDLVAAA ANLGRAAQFM YLDGDGNHSQ LHQRIASLLF
EPYA
