TPS2_LITCU
ID TPS2_LITCU Reviewed; 580 AA.
AC G0Y7D2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Alpha-thujene synthase, chloroplastic {ECO:0000303|Ref.1};
DE EC=4.2.3.- {ECO:0000269|Ref.1};
DE AltName: Full=Terpene synthase 2 {ECO:0000303|Ref.1};
DE Short=LcTPS2 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=TPS2 {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
CC (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 -!- 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 developing and mature fruits (Ref.1).
CC Barely detectable in 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; HQ651179; AEJ91555.1; -; mRNA.
DR SMR; G0Y7D2; -.
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: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..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..580
FT /note="Alpha-thujene synthase, chloroplastic"
FT /id="PRO_0000455073"
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; 67595 MW; 08376C5DAC4EB51D CRC64;
MALQLLTPSF SFQHSPSPHK LTTLRYTHHR IRCTASAPSY SDLVRRRSAN YKPSKWDSNF
VETLESDYKK ENHEMYIEKL MGDVKHLMKE VVNPIEKMEL VDTIQRLGLG YLFNKEIKEV
LNTITTSKAT LKTKKDLHAV ALQFRLLRQH GYEVSPDAFH EFKDEKGGFK ESLCMDIKGM
LCLYEASHLS FQGEVVLDEA REFTSTHLKA IGGNIDPVLL KKVRHSLEMP LHWRMLRLEA
RWYIETYDEE DRKNPSLAEL AKHDFNSVQT IYQRSLKRMS RWWRDLGLGE RLEFSRDRLV
ECFFWTTGVI FDPQFERCRG VLTKVNQLVS TIDDVYDVYG SLEELELFTD AVDRWDIRAM
EQLPEYMKIC YLALYNTTND IAYEALKEEG LDVIPYLKKV WTDLCKSYIV EARWYSNGYK
PTLEEYLENA WTSIAGPVAL VHAYFSFGQK MPFEALNYSN TSSLIKWSSM IFRLCDDLAT
SSDEVARGDV PKSIQCYMYE AGVSESVARD HIKYLIDEAW KKMNECLVYN TPFLQPLINA
GLNLARMAHC MYERGDGHGF SNELDKKRVL LLLAEPFKFM
