TPS2_LOTJA
ID TPS2_LOTJA Reviewed; 595 AA.
AC Q672F7;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Tricyclene synthase EBOS, chloroplastic;
DE EC=4.2.3.105;
DE AltName: Full=(E)-beta-ocimene synthase;
DE Short=LjEBOS;
DE Short=LjEbetaOS;
DE EC=4.2.3.106;
DE AltName: Full=Terpenoid synthase 2;
DE Short=LjTPS2;
DE Flags: Precursor;
GN Name=EBOS;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY TETRANYCHUS URTICAE;
RP WOUNDING AND ALAMETHICIN, AND CATALYTIC ACTIVITY.
RX PubMed=15310830; DOI=10.1104/pp.104.042929;
RA Arimura G., Ozawa R., Kugimiya S., Takabayashi J., Bohlmann J.;
RT "Herbivore-induced defense response in a model legume. Two-spotted spider
RT mites induce emission of (E)-beta-ocimene and transcript accumulation of
RT (E)-beta-ocimene synthase in Lotus japonicus.";
RL Plant Physiol. 135:1976-1983(2004).
CC -!- FUNCTION: Promotes the emission of terpenes volatile organic compounds
CC (VOC) in response to damage mediated by arthropod herbivores (e.g.
CC Tetranychus urticae), probably to attract natural enemies of the
CC herbivores. {ECO:0000269|PubMed:15310830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + tricyclene;
CC Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64266; EC=4.2.3.105;
CC Evidence={ECO:0000269|PubMed:15310830};
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;
CC Evidence={ECO:0000269|PubMed:15310830};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- INDUCTION: Accumulates in response to Tetranychus urticae (two-spotted
CC spider mites) infection, and transiently after mechanical wounding and
CC upon treatment with alamethicin (ALA), a potent fungal elicitor.
CC {ECO:0000269|PubMed:15310830}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AY575970; AAT86042.1; -; mRNA.
DR AlphaFoldDB; Q672F7; -.
DR SMR; Q672F7; -.
DR OMA; RICCAVS; -.
DR BRENDA; 4.2.3.106; 3076.
DR UniPathway; UPA00213; -.
DR GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
DR GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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; Manganese; Metal-binding; Plant defense;
KW Plastid; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..595
FT /note="Tricyclene synthase EBOS, chloroplastic"
FT /id="PRO_0000418164"
FT MOTIF 343..347
FT /note="DDXXD motif"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 595 AA; 68846 MW; F02C546492BCBA34 CRC64;
MAQSFSMVLN SSFTSHPIFC KPQKLIIRGH NLLQGHRINS PIPCYASTSS TSVSQRKSAN
YQPNIWNYDY LQSLKLGYAD AHYEDMAKKL QEEVRRIIKD DKAEIWTTLE LIDDVKRLGL
GYHFEKEIRE VLNKFLSLNT CVHRSLDKTA LCFRLLREYG SDVSADIFER FLDQNGNFKT
SLVNNVKGML SLYEASFLSY EGEQILDKAN AFTSFHLKSI HEEDINNILL EQVNHALELP
LHRRIHRLEA RWYTESYSRR KDANWVLLEA AKLDFNMVQS TLQKDLQEMS RWWKGMGLAP
KLSFSRDRLM ECFFWTVGMA FEPKYSDLRK GLTKVTSLIT TIDDIYDVHG TLEELELFTA
IVESWDIKAM QVLPEYMKIS FLALYNTVNE LAYDALREQG HDILPYLTKA WSDMLKAFLQ
EAKWCREKHL PKFEHYLNNA WVSVSGVVIL THAYFLLNHN TTKEVLEALE NYHALLKRPS
IIFRLCNDLG TSTAELQRGE VANSILSCMH ENDIGEESAH QHIHSLLNET WKKMNRDRFI
HSPFPEPFVE IATNLARIAQ CTYQTGDGHG APDSIAKNRV KSLIIEPIVL NGDIY
