TPS3_CANOD
ID TPS3_CANOD Reviewed; 547 AA.
AC A0A7G5KLV2;
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 TPS3 {ECO:0000305};
DE AltName: Full=Alpha-bergamotene synthase TPS3 {ECO:0000305};
DE EC=4.3.2.- {ECO:0000269|PubMed:25956881};
DE AltName: Full=Terpene synthase 3 {ECO:0000303|PubMed:25956881};
DE Short=CoTPS3 {ECO:0000303|PubMed:25956881};
GN Name=TPS3 {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 alpha-bergamotene
CC (PubMed:25956881). Does not use (2E)-geranyl diphosphate (GPP) as
CC substrate (PubMed:25956881). {ECO:0000269|PubMed:25956881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62756, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31428;
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. Tpsb subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MN230107; QMW48844.1; -; 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..547
FT /note="Sesquiterpene synthase TPS3"
FT /id="PRO_0000455180"
FT MOTIF 302..306
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:25956881"
FT BINDING 265
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 302
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 306
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 443
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 446
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 547 AA; 63739 MW; CD7AA4EEF01C78AF CRC64;
MNPVSLLSLS GERRSANWKP SSWDSNQIHQ SLKSDFNDLQ EKWHTELKQA VEQMLEAVAE
PLQKLTLIDD IQRLGVAYRF EKQIDDALSS IYSNYAAEVS SKKDLLAASL YFRLLRQHGC
YVSPDIFIQF KDEAGQFKAS LGDDVEGLLS LYEASYLGIK GETILDDAKA FSTSTLENLM
PHVEADIASR ISHALHLPLH WNMRRMEARL YIDVYRENKK RRNDNLLEFA RLDFNMLQVI
HQRDLKDVSF WWDFLDLPRK LGFIRDRLME SFIFSVGLNF EPQFSECRKA ATKDILLITV
LDDIYDIYGS MDEVEIFNNA VNRWDLGAVD ELPEYMQLCY LGLLNSVNEL AYVTMKDTGR
NVLDFLKKLW KRHFNAAVKE SRWFHRQYTP TLEEYMENAQ ISIGAPLVLT HAYVKMLKYM
PNEDVNHVDK YLKLISMMCY VFRLYDDWGT SKAEIERGDV PKAIQCYMHE AKVSEEIARE
HIKNIINERW KELNEECLKA TDLNRKFVAA VLDALRAAAF FYHDRDGFGE PDHKFKSQAM
ALFSQQV
