LNOL4_PERFR
ID LNOL4_PERFR Reviewed; 604 AA.
AC C0KWV7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Linalool synthase Tps-5042L13, chloroplastic {ECO:0000303|PubMed:20447664};
DE Short=PfTps-5042L {ECO:0000303|PubMed:20447664};
DE EC=4.2.3.- {ECO:0000269|PubMed:20447664};
DE Flags: Precursor;
GN Name=Tps-5042L13 {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. 5042;
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; FJ644548; ACN42013.2; -; 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..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..604
FT /note="Linalool synthase Tps-5042L13, chloroplastic"
FT /id="PRO_0000455256"
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; 70367 MW; 5AF6DF3D1349D93A CRC64;
MSSMRIYVAI MKKPSVKHVD NVDKKASKPS WRVSSSATAG LRASSSLQLD VKKPADEILT
ARRSGNYQPS LWDFNYLQPL NTTHYKEERH LKREAELIEQ VKMLLEEEME AVQQLELVDD
LKNLGLSYFF EDQIKQILTF IYNEHKCFRS NVEAEERDLY FTALGFRLLR QHGFQVSQEV
FDCFKNEEGS DFKASLGDDT KGLVQLYEAS FLLREGEDTL ELARQYATKF LQKKVDHELI
DDDNNLLSWI RHSLEIPLHW RIQRLEARWF LDAYATRHDV NPIILELAKL DFNIIQATQQ
EELKDLSRWW NSTCLAEKLP FVRDRLVESY FWAIALFEPH QYGYHRKIAA KIITLITSLD
DVYDIYGTLD ELQLFTDAIQ RWDTESISRL PYYMQLFYMV LYNFVSELAY DGLKEKGFIT
IPYLQRSWAD LVEAYLKEAK WFYNGYTPSM EEYLNNAYIS IGATPVISQV FFTLATSIDK
PVIESLYEYH RILRLSGMLV RLPDDLGTSP FEMKRGDVPK AILLYMKERN ATEIEAQEHV
RFLIREAWKE MNTATAAADC PLTDDLVAAA ANLGRAAQFM YLDGDGNHSQ LHQRIASLLF
EPYA
