TPS2_CANOD
ID TPS2_CANOD Reviewed; 561 AA.
AC A0A7G5KLV1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Sesquiterpene synthase TPS2 {ECO:0000305};
DE AltName: Full=Beta-copaene synthase TPS2 {ECO:0000305};
DE EC=4.2.3.127 {ECO:0000269|PubMed:25956881};
DE AltName: Full=Beta-cubebene synthase TPS2 {ECO:0000305};
DE EC=4.2.3.128 {ECO:0000269|PubMed:25956881};
DE AltName: Full=Beta-ylangene synthase TPS2 {ECO:0000305};
DE EC=4.2.3.- {ECO:0000269|PubMed:25956881};
DE AltName: Full=Terpene synthase 2 {ECO:0000303|PubMed:25956881};
DE Short=CoTPS2 {ECO:0000303|PubMed:25956881};
GN Name=TPS2 {ECO:0000303|PubMed:25956881};
OS Cananga odorata (Ylang-ylang tree) (Uvaria odorata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Annonaceae;
OC Ambavioideae; Cananga.
OX NCBI_TaxID=13393;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND MOTIF.
RX PubMed=25956881; DOI=10.1093/jxb/erv196;
RA Jin J., Kim M.J., Dhandapani S., Tjhang J.G., Yin J.L., Wong L.,
RA Sarojam R., Chua N.H., Jang I.C.;
RT "The floral transcriptome of ylang ylang (Cananga odorata var. fruticosa)
RT uncovers biosynthetic pathways for volatile organic compounds and a
RT multifunctional and novel sesquiterpene synthase.";
RL J. Exp. Bot. 66:3959-3975(2015).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile organic compounds (PubMed:25956881). Mediates the conversion
CC of (2E,6E)-farnesyl diphosphate (FPP) into beta-ylangene, beta-copaene
CC and beta-cubebene (PubMed:25956881). Does not use (2E)-geranyl
CC diphosphate (GPP) as substrate (PubMed:25956881).
CC {ECO:0000269|PubMed:25956881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-ylangene + diphosphate;
CC Xref=Rhea:RHEA:69775, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763,
CC ChEBI:CHEBI:188453; Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69776;
CC Evidence={ECO:0000269|PubMed:25956881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate;
CC Xref=Rhea:RHEA:33111, ChEBI:CHEBI:33019, ChEBI:CHEBI:64799,
CC ChEBI:CHEBI:175763; EC=4.2.3.127;
CC Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33112;
CC Evidence={ECO:0000269|PubMed:25956881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-cubebene + diphosphate;
CC Xref=Rhea:RHEA:32019, ChEBI:CHEBI:10363, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.128;
CC Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32020;
CC Evidence={ECO:0000269|PubMed:25956881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25956881}.
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|PubMed:25956881}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; MN230106; QMW48843.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..561
FT /note="Sesquiterpene synthase TPS2"
FT /id="PRO_0000455179"
FT REGION 6..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 314..318
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:25956881"
FT BINDING 277
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 318
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 455
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 458
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 561 AA; 65255 MW; A8C8EC01B5B96E77 CRC64;
MALIFANGHS DVPSTQPPIG KQKKEIGRES VNYHPSVWGD RFAILTAHEI EVDEITKQRA
EKLKHDVLKM LHNVSVSLQD LNLIDEIQRL GVGYHFETEI ENAMKRIYNS RDNDDDDLHA
VALRFRLLRQ HGYNVSSDVF KKFKDEKGEF KASLRENVRG LLSFYEAAYL GTADDTILDQ
AIDFTTDQLK SVLPNLNPPL SELVKLALDV PLHKRIERLQ SRYFISIYQE EKERNEVLLE
FAKLDFNVLQ SLHKEELSQL SRWWKDNDFA RKLPFIRDRL VECYFWILGV YYEPRYSRGR
MMTTKVISLT SIMDDTYDVY GKLDELELLT TAIERWEWAA MDELPDYMKL HFSALLTAVE
NFEEELSKEG KAYRISYFKN AYTKLAKAYL EEARWASADY VPTLEEYMKH AQVSSAYPVL
TLSSLLGMGA TATKEAFEWA INMPNAINAI SVVCRLKDDI TSAELEQQRV HVATAVECYI
KENGTTYEET CKLFKQKVDS AWKEINKEWM DPLQVPREII KRAVNFARVI EFLYRYKDMY
TESAGETKEC IAMVLVDRFV D
