TPS1_TOOSI
ID TPS1_TOOSI Reviewed; 595 AA.
AC I7GPX8; B6ZGQ4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Sesquiterpene synthase 1 {ECO:0000303|PubMed:23072391};
DE Short=TsTPS1 {ECO:0000303|PubMed:23072391};
DE AltName: Full=(4R)-limonene synthase TPS1, mitochondrial {ECO:0000303|PubMed:23072391};
DE EC=4.2.3.20 {ECO:0000269|PubMed:23072391};
DE Flags: Precursor;
GN Name=TPS1 {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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
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). Mediates
CC the conversion of (2E)-geranyl diphosphate (GPP) into (4R)-limonene
CC (PubMed:23072391). Can only use GPP as substrate, no activity with
CC farnesyl diphosphate (FPP) (PubMed:23072391).
CC {ECO:0000269|PubMed:23072391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4R)-limonene + diphosphate;
CC Xref=Rhea:RHEA:10940, ChEBI:CHEBI:15382, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.20;
CC Evidence={ECO:0000269|PubMed:23072391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10941;
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:23072391}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23072391}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rachis and leaflets
CC (PubMed:23072391). Accumulates particularly in glandular cells of the
CC leaf rachises (PubMed:23072391). {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; AB303572; BAH03282.1; -; mRNA.
DR EMBL; AB730584; BAM24404.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0034002; F:(R)-limonene 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:0046250; P:limonene biosynthetic process; IDA:UniProtKB.
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; 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 Lyase; Magnesium; Metal-binding; Mitochondrion; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..595
FT /note="Sesquiterpene synthase 1"
FT /id="PRO_0000454679"
FT MOTIF 348..352
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 484
FT /note="W -> C (in Ref. 1; BAH03282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 68911 MW; 10E996B757D34F78 CRC64;
MASHVLASLR SASARISTRL QSRSCILATA TSFSNGFVSA SLVQSMSTTT QCDESVARRS
ANYEPPIWTY DYVQSLRNPY AGGSYAKRIE KLKGDVRVML QKLVDLDPLH QLEFIDTLQR
LGVSYHYQEG IKGILDTVYN NYMQKQESLY AVALGFRLFR QHGYHIPADI FSSFRDDKGN
LKSCLGDDCR GILALYEAAH LLVEEERDIF YEIVNFTTAY LKEYVKHDND EYLSALVNHS
LEIPLHWRVL RLEARWFIGA YERAPNTHPI LLEFAKLDFN DVQATHQEDL KFMSRWWKNT
GLDREKMNFA RDRIVQNVLW SLGIIFEPQF AYCRRMSVKA YAFITLIDDV YDVYGTLDEL
ELFTDAVDRW DATAIEKLPD YMKPIFRTLY TSINDMALDA RKDRGVDTRP FLHKAWSTLF
NYYLMEAKWF SNGYMPTYKE YMDIAWFSVG GPVMIVHSYC AIANPATKEN MEFFQEYYDI
IRLWSTILRF KDDMGTSSDE LKRGDNPKSI QCYMHESGVS EKEARQHLGN LITETWMKVN
KNRAENPHLS DVYMGIAINM ARMALCMYQF GDGHAVEAHS KDRVLSLLIN PIPCP
