TPS2_TOOSI
ID TPS2_TOOSI Reviewed; 556 AA.
AC I7H727; E5RM29;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Sesquiterpene synthase 2 {ECO:0000303|PubMed:23072391};
DE Short=TsTPS2 {ECO:0000303|PubMed:23072391};
DE AltName: Full=Alpha-humulene synthase TPS2 {ECO:0000303|PubMed:21818683, ECO:0000303|PubMed:23072391};
DE EC=4.2.3.104 {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391};
DE AltName: Full=Alpha-selinene synthase TPS2 {ECO:0000303|PubMed:23072391};
DE EC=4.2.3.198 {ECO:0000269|PubMed:23072391};
DE AltName: Full=Beta-elemene synthase TPS2 {ECO:0000303|PubMed:23072391};
DE EC=4.2.3.- {ECO:0000269|PubMed:23072391};
DE AltName: Full=Delta-cadinene synthase TPS2 {ECO:0000303|PubMed:23072391};
DE EC=4.2.3.- {ECO:0000269|PubMed:23072391};
GN Name=TPS2 {ECO:0000303|PubMed:23072391};
OS Toona sinensis (Chinese mahogany) (Cedrela sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Meliaceae; Toona.
OX NCBI_TaxID=443222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND TISSUE SPECIFICITY.
RX PubMed=23072391; DOI=10.2174/138920112804724864;
RA Hsu C.-Y., Huang P.-L., Chen C.-M., Mao C.-T., Chaw S.-M.;
RT "Tangy scent in Toona sinensis (Meliaceae) leaflets: isolation, functional
RT characterization, and regulation of TsTPS1 and TsTPS2, two key terpene
RT synthase genes in the biosynthesis of the scent compound.";
RL Curr. Pharm. Biotechnol. 13:2721-2732(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND GENE FAMILY.
RX PubMed=21818683; DOI=10.1007/s11103-011-9813-x;
RA Bleeker P.M., Spyropoulou E.A., Diergaarde P.J., Volpin H., De Both M.T.J.,
RA Zerbe P., Bohlmann J., Falara V., Matsuba Y., Pichersky E., Haring M.A.,
RA Schuurink R.C.;
RT "RNA-seq discovery, functional characterization, and comparison of
RT sesquiterpene synthases from Solanum lycopersicum and Solanum habrochaites
RT trichomes.";
RL Plant Mol. Biol. 77:323-336(2011).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds known for their medicinal efficacy for treating
CC enteritis, dysentery, itch and some cancers (PubMed:23072391,
CC PubMed:21818683). Mediates the conversion of (2E,6E)-farnesyl
CC diphosphate (FPP) into beta-elemene, alpha-humulene, delta-cadinene and
CC alpha-selinene (PubMed:23072391, PubMed:21818683).
CC {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.104;
CC Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
CC Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:23072391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate;
CC Xref=Rhea:RHEA:47052, ChEBI:CHEBI:33019, ChEBI:CHEBI:59961,
CC ChEBI:CHEBI:175763; EC=4.2.3.198;
CC Evidence={ECO:0000269|PubMed:23072391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47053;
CC Evidence={ECO:0000269|PubMed:23072391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate;
CC Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:23072391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557;
CC Evidence={ECO:0000269|PubMed:23072391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,2S,4R)-beta-elemene +
CC diphosphate; Xref=Rhea:RHEA:68712, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62855, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:23072391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68713;
CC Evidence={ECO:0000269|PubMed:23072391};
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|PubMed:21818683, ECO:0000269|PubMed:23072391}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and mature leaflets and,
CC to a lower extent, in rachis and developing leaflets.
CC {ECO:0000269|PubMed:23072391}.
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:0000250|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; AB509224; BAJ46125.1; -; mRNA.
DR EMBL; AB730585; BAM24405.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0102889; F:beta-elemene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene 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; 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 SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..556
FT /note="Sesquiterpene synthase 2"
FT /id="PRO_0000454680"
FT MOTIF 309..313
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 113
FT /note="S -> I (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..165
FT /note="PGV -> LGA (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> K (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..305
FT /note="TIAMG -> IIAMA (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="P -> R (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="Q -> L (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="A -> V (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="H -> R (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="G -> A (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..449
FT /note="GTIA -> ETIS (in Ref. 1; BAJ46125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 64552 MW; 483474D2F86EED08 CRC64;
MSVPVSQIPS LKAKGVIMRR NANYHPNIWG DRFINYVPVD KMNHTCHLQA IEELKDAVRR
ELLTATGLSQ LNLIDAIQRL GVGYHFEREL EEALQHVYHK NHYHDDTEDN LYSISLRFRL
LRQHGYYVSC DILNKFKDEK DNFKESLTTD VPGMLSLYEA AHPGVHGEDI LDEAIAFTTT
HLKSLAIDHL RNPSLASQVI HALRQPLHRG VPRLENRRYI SIYQDEVSHN KALVKLFKLD
FNLVQSLHKK ELSEISRWWK ELDLANKLPF ARDRLVECYF WIIGVYYEPQ YSLARKILTK
TIAMGSIIDD IYDVYGTPEE LNLFTDAIER WDASCMDQLP EYMQIFYEAL LDLYNEIEKE
IAKEGWSYRV HYAKEAMKIL ARGYHDESKW FHNNYIPTME EYMHVALVTS GYTMLTTSSF
LGMDNIVTKE TFDWVFSGPK IIRASGTIAR LMDDVKSHKF EQERGHAASA VECYMEQHGV
SEQEVCKEFY QQVGNAWKDI NQDFLKPTDV PMTILMRVLN LARVIDVVYK EGDGYTHVGK
VMKENVASLL IDPIPV
