TS14A_SOLHA
ID TS14A_SOLHA Reviewed; 554 AA.
AC G8H5M9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Sesquiterpene synthase 14a {ECO:0000303|PubMed:21818683};
DE Short=ShTPS14a {ECO:0000303|PubMed:21818683};
DE AltName: Full=(E)-beta-farnesene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.47 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-gamma-bisabolene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.59 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(Z)-alpha-bisabolene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=(Z)-beta-farnesene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-acoradiene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-bisabolene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-myrcene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Limonene synthase TPS14a {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
GN Name=TPS14a {ECO:0000303|PubMed:21818683};
OS Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
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=62890;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. PI127826;
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, beta-
CC farnesene, (E)-gamma-bisabolene, beta-acoradiene, selinene and (Z)-
CC alpha-bisabolene (PubMed:21818683). Low or no activity with (2Z,6Z)-
CC farnesyl diphosphate ((ZZ)-FPP) (PubMed:21818683). Can act with a low
CC efficiency as a monoterpene synthase with geranyl diphosphate (GPP) as
CC substrate, thus producing beta-myrcene and limonene (PubMed:21818683).
CC {ECO:0000269|PubMed:21818683}.
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:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (Z)-alpha-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:68532, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49241, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68533;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-acoradiene + diphosphate;
CC Xref=Rhea:RHEA:68520, ChEBI:CHEBI:33019, ChEBI:CHEBI:172925,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68521;
CC Evidence={ECO:0000269|PubMed:21818683};
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:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28299;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (Z)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:68508, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:39242, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68509;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + limonene;
CC Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:21818683};
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 stem trichomes.
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; JN402390; AEM23827.1; -; mRNA.
DR UniPathway; UPA00213; -.
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.
FT CHAIN 1..554
FT /note="Sesquiterpene synthase 14a"
FT /id="PRO_0000454684"
FT MOTIF 305..309
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
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 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 554 AA; 64973 MW; 6306060CF0AC9CA5 CRC64;
MNQLAMVNTT ITRPLANYHS SVWGNYFLSY TPQLTETSSQ EKRELEELKE KVRQMLVETP
DNSTQKLVLI DTIQRLGVAY HFENHIKISI QNIFDEFEKN KNKDNDDDLC VVALRFRLVR
GQRHYMSSDV FTRFTNDDGK FKETLTKDVS GLLNLYEATH LRVHGEEILE DALSFTVTHL
KSMSPKLDNS LKAQVSEALF QPIHTNIPRV VARKYIRIYE NIESHDDLLL KFAKLDFHIL
QKMHQRELSE LTRWWKYLDY ENKYPYARDK LVECYFWATG VYFGPQYKRA RKTLTKLIVI
ITITDDLYDA YATYDELVPY TDAVERCEIS AMHSISPYMR PLYQVFLDYF DEMEKELTKD
GKAHYVYYAK IETNKWIKSY LKEAEWLKND IIPKCEEYKR NATITVSSQM ILITCLIVAG
EFISKETFEW MINESLIAPA SSLINRLKDD IIGHEHEQQR EHGASFIECY VKEYRASKQE
AYVEARRQIA NAWKDINTDY LHATQVPTFV LEPALNLSRL VDILQEDDFT DSQNFLKDTI
TLLFVDSVNS TSCG
