TPS1_LITCU
ID TPS1_LITCU Reviewed; 582 AA.
AC G0Y7D1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Trans-ocimene synthase, chloroplastic {ECO:0000303|Ref.1};
DE Short=(E)-beta-ocimene synthase {ECO:0000303|Ref.1};
DE EC=4.2.3.106 {ECO:0000269|Ref.1};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|Ref.1};
DE Short=LcTPS1 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=TPS1 {ECO:0000303|Ref.1};
OS Litsea cubeba (Aromatic litsea) (Laurus cubeba).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Litsea.
OX NCBI_TaxID=155299;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX DOI=10.1007/s11295-011-0377-3;
RA Chang Y.-T., Chu F.-H.;
RT "Molecular cloning and characterization of monoterpene synthases from
RT Litsea cubeba (Lour.) Persoon.";
RL Tree Genet. Genomes 7:835-844(2011).
CC -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC monoterpene natural products used by traditional Chinese medicine to
CC treat headache, inflammation and intoxication (Ref.1). Catalyzes the
CC conversion of (2E)-geranyl diphosphate (GPP) into (E)-beta-ocimene
CC (Ref.1). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64280; EC=4.2.3.106; Evidence={ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
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|Ref.1}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in male and female leaves (Ref.1). Barely
CC detectable in fruits and shoots (Ref.1). {ECO:0000269|Ref.1}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ651178; AEJ91554.1; -; mRNA.
DR BRENDA; 4.2.3.106; 12979.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:UniProtKB.
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:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043693; P:monoterpene 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..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..582
FT /note="Trans-ocimene synthase, chloroplastic"
FT /id="PRO_0000455072"
FT MOTIF 333..337
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 582 AA; 67150 MW; 1A8B29639A3F3C38 CRC64;
MSLIIQSLPH WSRIPPRPPQ LSQFQNSSRP KPLIQAGQVQ HNALQIARRS ANYHPSIWDP
QYIESLKSPY GDECFGTRLE KLKFEAKRLL EATIEPLSWL ELVDSIQRLG VAYHFEDEIK
EGLDGVYGVG AHAGDDLYTA ALQFRLLRQH GYGVTPDIFN KFLEKERTFK ACTSLDAKGL
LSLYEASHTM IHGEEVLEDA KEFSVKHLNY LMGNLQNNLR EQVQHALEMP LHWRMPRLEA
KHYIDVNGRS DERNMVLLEL ARLDFNFVQS KHQEELKEVS RWWRDLGLAK KLGFSRDRLV
ENYLWAVGIA PEPKFSNCRK GLTKLISILT VIDDIYDVYG SLDELELFTE AVKRWDIEAL
ETLPEYMKIC YLALFNFVHE VSYDTLKDYG WNILPFIREE WERLCMSYLV EAEWFGNGNK
PALDEYLRNG WISVGGPVAM VHAYFLQGRP IRKDSINFLD HGSELIYWSS VATRLNDDLG
TSKAEMKRGD VPKAVECYMI QTGESYEDAR EHIQGLVRDC WKKMNEECLK CCLPKSYVET
VLNMVRTAQC IYQHGDGIGT STGVTQDRVI SLICEPVPSQ WP
