TS14B_SOLHA
ID TS14B_SOLHA Reviewed; 554 AA.
AC G8H5N1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Sesquiterpene synthase 14b {ECO:0000303|PubMed:21818683};
DE Short=ShTPS14b {ECO:0000303|PubMed:21818683};
DE AltName: Full=(+)-thujopsene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.79 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-alpha-bisabolene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-beta-farnesene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.47 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-gamma-bisabolene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.59 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(Z)-beta-farnesene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Alpha-acoradiene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Alpha-cederene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-acoradiene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-bisabolene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-myrcene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Limonene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Terpinolene synthase TPS14b {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.113 {ECO:0000269|PubMed:21818683};
GN Name=TPS14b {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, AND GENE
RP FAMILY.
RC STRAIN=cv. PI126449;
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 (+)-thujopsene, beta-
CC bisabolene, alpha-cederene, beta-acoradiene, (E)-gamma-bisabolene, (Z)-
CC alpha-bisabolene, (Z)-beta-farnesene and (E)-beta-farnesene, and of
CC (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into (E)-gamma-bisabolene, (E)-
CC alpha-bisabolene, (E)-beta-farnesene, (Z)-beta-farnesene, beta-
CC bisabolene, beta-acoradiene and alpha-acoradiene (PubMed:21818683). Can
CC act with a low efficiency as a monoterpene synthase with geranyl
CC diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene
CC and terpinolene (PubMed:21818683). {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=(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:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469;
CC Evidence={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:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68473;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:68504, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:39242, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68505;
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 = (+)-thujopsene + diphosphate;
CC Xref=Rhea:RHEA:30375, ChEBI:CHEBI:33019, ChEBI:CHEBI:61737,
CC ChEBI:CHEBI:175763; EC=4.2.3.79;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30376;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:68544, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68545;
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=(2Z,6Z)-farnesyl diphosphate = beta-acoradiene + diphosphate;
CC Xref=Rhea:RHEA:68516, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374,
CC ChEBI:CHEBI:172925; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68517;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = alpha-acoradiene + diphosphate;
CC Xref=Rhea:RHEA:68512, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374,
CC ChEBI:CHEBI:172926; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68513;
CC Evidence={ECO:0000269|PubMed:21818683};
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:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-alpha-cedrene +
CC diphosphate; Xref=Rhea:RHEA:68536, ChEBI:CHEBI:10216,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68537;
CC Evidence={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 = 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=(2Z,6Z)-farnesyl diphosphate = (-)-alpha-cedrene +
CC diphosphate; Xref=Rhea:RHEA:68540, ChEBI:CHEBI:10216,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68541;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.113;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
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 -!- 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; JN402392; AEM23829.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..554
FT /note="Sesquiterpene synthase 14b"
FT /id="PRO_0000454685"
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; 65036 MW; 863D6F4D56FD8FE0 CRC64;
MNQLAMVNTT ITRPLANYHS SVWGNYFLSY TPQLTEISSQ EKRELEELKE KVRQMLVETP
DNSTQKLVLI DTIQRLGVAY HFENHIKISI QNIFDEFEKN KNKDNDDDLC VVALRFRLVR
GQRHYMSSDV FTRFTNDDGK FKETLTKDVQ GLLNLYEATH LRVHGEEILE EALSFTVTHL
KSMSPKLDNS LKAQVSEALF QPIHTNIPRV VARKYIRIYE NIESHDDLLL KFAKLDFHIL
QKMHQRELSE LTRWWKDLDH SNKYPYARDK LVECYFWAIG VYFGPQYKRA RRTLTKLIVI
ITITDDLYDA YATYDELVPY TNAVERCEIS AMHSISPYMR PLYQVFLDYF DEMEEELTKD
GKAHYVYYAK IETNKWIKSY LKEAEWLKND IIPKCEEYKR NATITISNQM NLITCLIVAG
EFISKETFEW MINESLIAPA SSLINRLKDD IIGHEHEQQR EHGASFIECY VKEYRASKQE
AYVEARRQIT NAWKDINTDY LHATQVPTFV LEPALNLSRL VDILQEDDFT DSQNFLKDTI
TLLFVDSVNS TSCG
