TPS14_SOLLC
ID TPS14_SOLLC Reviewed; 568 AA.
AC G5CV54;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Sesquiterpene synthase 14 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE Short=SlTPS14 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE Short=Terpene synthase 14 {ECO:0000303|PubMed:21813655};
DE AltName: Full=(E)-gamma-bisabolene synthase TPS14 {ECO:0000303|PubMed:21813655};
DE EC=4.2.3.59 {ECO:0000269|PubMed:21813655};
DE AltName: Full=(Z)-gamma-bisabolene synthase TPS14 {ECO:0000303|PubMed:21813655};
DE EC=4.2.3.40 {ECO:0000269|PubMed:21813655};
DE AltName: Full=Alpha-bisabolene synthase TPS14 {ECO:0000303|PubMed:21813655};
DE EC=4.2.3.- {ECO:0000269|PubMed:21813655};
DE AltName: Full=Beta-bisabolene synthase TPS14 {ECO:0000303|PubMed:21813655};
DE EC=4.2.3.- {ECO:0000269|PubMed:21813655};
GN Name=TPS14 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. M82;
RX PubMed=21813655; DOI=10.1104/pp.111.179648;
RA Falara V., Akhtar T.A., Nguyen T.T.H., Spyropoulou E.A., Bleeker P.M.,
RA Schauvinhold I., Matsuba Y., Bonini M.E., Schilmiller A.L., Last R.L.,
RA Schuurink R.C., Pichersky E.;
RT "The tomato terpene synthase gene family.";
RL Plant Physiol. 157:770-789(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Moneymaker;
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 (PubMed:21818683). Mediates the conversion of
CC (2E,6E)-farnesyl diphosphate ((EE)-FPP) into beta-bisabolene, and of
CC (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into alpha-bisabolene, but also
CC smaller amounts of (Z)-gamma-bisabolene, (E)-gamma-bisabolene and
CC nerolidol (PubMed:21813655). {ECO:0000269|PubMed:21813655,
CC ECO:0000269|PubMed:21818683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-alpha-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:68472, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49242, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21813655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68473;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate;
CC Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249,
CC ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21813655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate;
CC Xref=Rhea:RHEA:68528, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21813655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (Z)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:26081, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49238, ChEBI:CHEBI:175763; EC=4.2.3.40;
CC Evidence={ECO:0000269|PubMed:21813655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26082;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:28298, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49239, ChEBI:CHEBI:175763; EC=4.2.3.59;
CC Evidence={ECO:0000269|PubMed:21813655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28299;
CC Evidence={ECO:0000269|PubMed:21813655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:68468, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49239, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21813655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469;
CC Evidence={ECO:0000269|PubMed:21813655};
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}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, to a lower extent in
CC flowers and, at low levels, in fruits. {ECO:0000269|PubMed:21813655,
CC ECO:0000269|PubMed:21818683}.
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; JN412091; AEP82782.1; -; Genomic_DNA.
DR RefSeq; NP_001318113.1; NM_001331184.1.
DR SMR; G5CV54; -.
DR STRING; 4081.Solyc09g092470.2.1; -.
DR PaxDb; G5CV54; -.
DR PRIDE; G5CV54; -.
DR EnsemblPlants; Solyc09g092470.2.1; Solyc09g092470.2.1; Solyc09g092470.2.
DR GeneID; 101249861; -.
DR Gramene; Solyc09g092470.2.1; Solyc09g092470.2.1; Solyc09g092470.2.
DR KEGG; sly:101249861; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; G5CV54; -.
DR OMA; YYAKERM; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; G5CV54; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Chromosome 9.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid 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; Reference proteome.
FT CHAIN 1..568
FT /note="Sesquiterpene synthase 14"
FT /id="PRO_0000454691"
FT MOTIF 319..323
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 568 AA; 66548 MW; 97764A0153E669A5 CRC64;
MATNLTLETD KEIKNMNQLS MIDTTITRPL ANYHSSVWKN YFLSYTPQLT EISSQEKLEL
EELKEKVRQM LVETSDKSTQ KLVLIDTIQR LGVAYHFDNE IKISIQNIFD EFEQNKNEDD
NDLYIVALRF RLVRGQRHYM SSDVFKKFTN DDGKFKETLT KDVQGLLNLY EATHLRVHGE
QILEEALSFT VTHLKSMSPK LDSSLKAQVS EALIQPIYTN VPRVVAPKYI RIYENIESHD
DLLLKFVKLD FHILQKMHQR ELSELTRWWK DLDHSNKYPY ARDKLVECYF WATGVYFGPQ
YKRARRMITK LIVIITITDD LYDAYATYDE LVPYTNAVER CEISAMDSIS PYMRPLYQVF
LDYFDEMEEE LTKDGKAHYV YYAKVEMNKL IKSYLKEAEW LKNDIIPKCE EYKRNATITV
ANQMILITCL IVAGEFISKE TFEWMINESL IAPASSLINR LKDDIIGHEH EQQREHGASF
VECYVKEYRA SKQEAYVEAR RQIANAWKDI NTDYLHATQV PTFVLQPALN LSRLVDILQE
DDFTDSQNFL KDTIKLLFVD SVNSTSCG
