TPS3_LITCU
ID TPS3_LITCU Reviewed; 580 AA.
AC G0Y7D3;
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=Alpha-thujene synthase TPS3, chloroplastic {ECO:0000303|Ref.1};
DE EC=4.2.3.- {ECO:0000269|Ref.1};
DE AltName: Full=(+)-sabinene synthase TPS3 {ECO:0000303|Ref.1};
DE EC=4.2.3.110 {ECO:0000269|Ref.1};
DE AltName: Full=Terpene synthase 3 {ECO:0000303|Ref.1};
DE Short=LcTPS3 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=TPS3 {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 alpha-thujene and
CC (1R,5R)-sabinene (Ref.1). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-thujene + diphosphate;
CC Xref=Rhea:RHEA:68644, ChEBI:CHEBI:33019, ChEBI:CHEBI:50031,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68645;
CC Evidence={ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-sabinene + diphosphate;
CC Xref=Rhea:RHEA:32547, ChEBI:CHEBI:33019, ChEBI:CHEBI:50029,
CC ChEBI:CHEBI:58057; EC=4.2.3.110; Evidence={ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32548;
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: Mostly expressed in developing and mature fruits,
CC and, to a lower extent, in male leaves (Ref.1). Barely detectable in
CC female leaves 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}.
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DR EMBL; HQ651180; AEJ91556.1; -; mRNA.
DR BRENDA; 4.2.3.110; 12979.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102700; F:alpha-thujene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0080015; F:sabinene synthase activity; IDA:UniProtKB.
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..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..580
FT /note="Alpha-thujene synthase TPS3, chloroplastic"
FT /id="PRO_0000455074"
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 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 580 AA; 67406 MW; 743AE5C5517DC359 CRC64;
MALQLLTPSF SFQHSPSPHR LTTLRYTHHT IRCTASAPSY SDLVGRRSAN YKPSKWDSNF
VETLESDYKK ENHEMYIEKL MGDVKHLMKK VVNPIEKMEL VDTIQRLGLG YLFNKEIKEV
LNTIATSKAT FKTKKDLHAV ALQFRLLRQH GYEVSPDAFH KFKDEKGGFK ESLCMDIKGM
LSLYEASHLS FQGEVVLDEA REFTSTHLKA IEGNIDPVLL KKVRHSLEMP LHWRMLRLEA
RWYIETYDEE DRKNPSLAEL AKHDFNSVQT IYQRSLKRMS RWWRDLGLGE RLEFSRDRLV
ECFFWTTGVI FDPQFERCRG VLTKVNQLVS TIDDVYDVYG SLEELELFTD AVDRWDIRAM
EQLPEYMKIC YLALYNTTND IAYEALKEEG LDVIPYLKKV WTDLCKSYIV EARWYSNGYK
PTLEEYLENA WTSIAGPVAL GHAYFSFGQK MPFEALNYSN TSSLIKWSSM IFRLCDDLAT
SSDEVARGDV PKSIQCYMYE AGVSESVARD HIKYLIDEAW KKMNECLVPS TPFLQPLINA
GFNLARMAHC MYEHGDGHGF SNELDKKRVL LLLAEPFKFM
