TPS3_XANST
ID TPS3_XANST Reviewed; 559 AA.
AC A0A0D4D912;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Sesquiterpene synthase TPS3 {ECO:0000305};
DE AltName: Full=Germacrene A synthase {ECO:0000303|PubMed:26858282};
DE EC=4.2.3.23 {ECO:0000269|PubMed:26858282};
DE AltName: Full=Terpene synthase 3 {ECO:0000303|PubMed:26858282};
DE Short=XsTPS3 {ECO:0000303|PubMed:26858282};
GN Name=TPS3 {ECO:0000303|PubMed:26858282}; Synonyms=GAS {ECO:0000303|Ref.1};
OS Xanthium strumarium (Rough cocklebur).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Xanthium.
OX NCBI_TaxID=318068;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Trichome gland;
RA Chen F.F., Zhang Y.S.;
RT "Xanthium strumarium germacrene A synthase (GAS) mRNA.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MOTIF.
RX PubMed=26858282; DOI=10.1093/pcp/pcw019;
RA Li Y., Chen F., Li Z., Li C., Zhang Y.;
RT "Identification and functional characterization of sesquiterpene synthases
RT from Xanthium strumarium.";
RL Plant Cell Physiol. 57:630-641(2016).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds (PubMed:26858282). Mediates the conversion of
CC (2E,6E)-farnesyl diphosphate (FPP) into (+)-(R)-germacrene A
CC (PubMed:26858282). {ECO:0000269|PubMed:26858282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-(R)-germacrene A +
CC diphosphate; Xref=Rhea:RHEA:12516, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:41595, ChEBI:CHEBI:175763; EC=4.2.3.23;
CC Evidence={ECO:0000269|PubMed:26858282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12517;
CC Evidence={ECO:0000269|PubMed:26858282};
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:0000250|UniProtKB:Q6Q3H2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in glandular trichomes
CC (PubMed:26858282). Expressed in roots and leaves (PubMed:26858282).
CC {ECO:0000269|PubMed:26858282}.
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:26858282}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa 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; KJ194511; AJT60315.1; -; mRNA.
DR SMR; A0A0D4D912; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034005; F:germacrene-A synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0046246; P:terpene biosynthetic process; IEA:UniProt.
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..559
FT /note="Sesquiterpene synthase TPS3"
FT /id="PRO_0000455108"
FT MOTIF 312..316
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:26858282"
FT BINDING 275
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
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="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 559 AA; 64560 MW; B3D45267E861823E CRC64;
MAAVGANATL LTNTKSTVEP VRPLANFPPS VWGDMFLSFS LDNSKMEEYA KAMEKPKQEV
RRLILDPTMD SNKKLSLIYV VHRLGLTYMF LKEIEGQLDR LFEEFNLEDY VDVDLHTISI
NFQAFRHLGY KLPCDVFNKF KNNDSNAFKE SIASDVRGLL GLYESAQLRV KGEKILDDAS
AFAETKLKSL VNTLEGSLAQ QVKQALKRPF HQGMPMVEAR LYFTNYQEEF SKYDSLLKLA
KLHFNYLQLQ QKEELRIVSK WWKDMRFQET TPYIRDRVPE IYLWILGLYF EPKYSLARII
ATKITLFLVV LDDTYDAYGT LEELRLLTHA INRWDMRAMS DIPEYIRPFY KILLDEYAEL
EKQLAKEGRL KSVIASKEAF QDIARGYIEE AEWTNSGYVA SFPEYMKNGL ITSAYNVISK
SALVGMGEVV SADALAWYES HPKILQASEL ISRLQDDVMT YQFERERGQS ATGVDSYIKT
YGVSEKEAIE ELKKMIENAW KDINEGCLKP REVSMDLLAP ILNLARMIDV VYRYDDGFTF
PGKTLKEYIT LLFVDSLPM
