TPS4_MEDTR
ID TPS4_MEDTR Reviewed; 580 AA.
AC Q5UB07; B7FLI6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Tricyclene synthase TPS4, chloroplastic;
DE EC=4.2.3.105;
DE AltName: Full=(E)-beta-ocimene synthase;
DE Short=MtEBOS;
DE Short=MtEbetaOS;
DE EC=4.2.3.106;
DE AltName: Full=Terpenoid synthase 4;
DE Short=MtTPS4;
DE Flags: Precursor;
GN Name=TPS4;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY WOUNDING; JASMONIC ACID
RP AND LEPIDOPTERAN HERBIVORES, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Jemalong A17; TISSUE=Leaf;
RX PubMed=15660362; DOI=10.1002/arch.20037;
RA Gomez S.K., Cox M.M., Bede J.C., Inoue K., Alborn H.T., Tumlinson J.H.,
RA Korth K.L.;
RT "Lepidopteran herbivory and oral factors induce transcripts encoding novel
RT terpene synthases in Medicago truncatula.";
RL Arch. Insect Biochem. Physiol. 58:114-127(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490.
RA Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.;
RT "Medicago truncatula full length cDNA cloning project.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Jemalong A17;
RX PubMed=19249223; DOI=10.1016/j.plaphy.2009.01.008;
RA Navia-Gine W.G., Yuan J.S., Mauromoustakos A., Murphy J.B., Chen F.,
RA Korth K.L.;
RT "Medicago truncatula (E)-beta-ocimene synthase is induced by insect
RT herbivory with corresponding increases in emission of volatile ocimene.";
RL Plant Physiol. Biochem. 47:416-425(2009).
CC -!- FUNCTION: Promotes the emission of terpenes volatile organic compounds
CC (VOC) in response to damage mediated by arthropod herbivores (e.g.
CC Spodoptera exigua), probably to attract natural enemies of the
CC herbivores. {ECO:0000269|PubMed:15660362, ECO:0000269|PubMed:19249223}.
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:19249223};
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:19249223};
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
CC {ECO:0000269|PubMed:15660362}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:19249223}.
CC -!- INDUCTION: Accumulates in response to wounding, methyl jasmonate (meJA)
CC and infection by Spodoptera exigua (beet armyworm), a lepidopteran
CC herbivory. Also induced by lepidopteran oral secretions.
CC {ECO:0000269|PubMed:15660362}.
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; AY766248; AAV36465.1; -; mRNA.
DR EMBL; BT052958; ACJ85620.1; -; mRNA.
DR AlphaFoldDB; Q5UB07; -.
DR SMR; Q5UB07; -.
DR PRIDE; Q5UB07; -.
DR KEGG; ag:AAV36465; -.
DR BRENDA; 4.2.3.106; 3201.
DR UniPathway; UPA00213; -.
DR GO; GO:0009570; C:chloroplast stroma; IDA: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:0009753; P:response to jasmonic acid; 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..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..580
FT /note="Tricyclene synthase TPS4, chloroplastic"
FT /id="PRO_0000418165"
FT MOTIF 334..338
FT /note="DDXXD motif"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 84
FT /note="K -> R (in Ref. 2; ACJ85620)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> T (in Ref. 2; ACJ85620)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="T -> N (in Ref. 2; ACJ85620)"
FT /evidence="ECO:0000305"
FT CONFLICT 485..490
FT /note="AELERG -> VKKKKK (in Ref. 2; ACJ85620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 67120 MW; 83F420EB98E09FCE CRC64;
MLLNSSFISL PSFFKSQELG RTNLLIHRNG SPLLCYATNT NVSQRKSANY QPNIWNYDIL
QSLKHDYEDA RYVDRSRRLQ EEVKRMIKDE NVNILELIDT VKQLGLSYHF EEEIGEALDR
FLSLEKCSGR NNFGRSLHET ALRFRLLREY GYDISPDIFE KFKDHNGNFK ACLVQDIKGM
LSLYDASFLS YEGEQILDEA NAFTSIHLKD LSEGRSSILI DQVNHSLELP LYRRVQSLEA
RWFIDSYENR KDANKVLLEA AKLNFNIVQS TLQQDLKEMS RWWKGMGLAP RLSFGRDRLM
ECFFWAAGMT PFEPQFSNIR KGLTKVCSLI TLIDDIYDVY GTLDELELFT TAVESWDINA
IQILPEYMKI FFLALYTTVN DFTYDTIKET GHDILPYLVK VWSDMLKAFL QEAKWCHNKH
MPKFDDYLNN AWVSVSGVVL LTHSYFLLNR NITKEGLGYL ENCPMLLQTP SIIFRLCNDL
ATSSAELERG EGANSIICYM NENGVSEEVA YKHIQNLLDQ TWKKMNKDRV INSPSSKYFS
ETIINLARIS HCTYQYGDGH GAPDTLAKNR IKALILEPIN
