TPS9_SOLHA
ID TPS9_SOLHA Reviewed; 544 AA.
AC G8H5M7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Terpene synthase 9 {ECO:0000303|PubMed:21818683};
DE Short=ShTPS9 {ECO:0000303|PubMed:21818683};
DE AltName: Full=(1E,4E)-germacrene B synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.71 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Alpha-humulene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-myrcene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Germacrene A synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Limonene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Terpinolene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.113 {ECO:0000269|PubMed:21818683};
GN Name=TPS9 {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. 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 (FPP) into (1E,4E)-germacrene B, but also
CC smaller amounts of germacrene A and C, and of (2Z,6Z)-farnesyl
CC diphosphate ((ZZ)-FPP) into alpha-humulene, germacrene A and germacrene
CC B (PubMed:21818683). Can act with a low efficiency as a monoterpene
CC synthase with geranyl diphosphate (GPP) as substrate, thus producing
CC beta-myrcene, limonene and terpinolene (PubMed:21818683).
CC {ECO:0000269|PubMed:21818683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1E,4E)-germacrene B +
CC diphosphate; Xref=Rhea:RHEA:25444, ChEBI:CHEBI:5337,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.71;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25445;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = diphosphate + germacrene A;
CC Xref=Rhea:RHEA:68776, ChEBI:CHEBI:33019, ChEBI:CHEBI:36517,
CC ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68777;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:68780, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68781;
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; JN402388; AEM23825.1; -; 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..544
FT /note="Terpene synthase 9"
FT /id="PRO_0000454682"
FT MOTIF 296..300
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 300
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"
SQ SEQUENCE 544 AA; 63794 MW; 832652FCE8B05477 CRC64;
MAASSANKSR PLANFHPTVW GYHFLSYTHE ITNQEKVEVD EYKETIRKML VEAPEGSEQK
LVLIDAMQRL GVAYHFHNEI ETSIQNIFDA PKQNNNLHIV SLHFRLVRQQ GHYMSSDVFK
QFTNQDGKFK ERLTNDVQGL LSLYEASYLR VRDEEILEEA LAFTTTHLKS IVSNMSNNNN
SLKVEVSEAL TQPIRMTLPR MEARRYISIY ENNDAHNHLL LKFAKLDFNM LQKLHQRELS
DLTRWWKDLD FANKYPYARD RLVECYFWIL GVYFEPKYSR ARKMMTKVLK MTSIIDDTFD
AYATFDELEP FNDAIQRWDA NAIDSIQPYM RPAYQAFLDI YSEMEQVLSK EGKLDRVYYA
KNEMKKLVRA YFKETQWLND CDHIPKYEEH MENSLVSGGY MMIPTTCLVG MEEFISIETF
EWLMNDPLIV RASSLIARAM NDIVGHEVEQ ERGHVASLIE CYMKDYGASK QEAYAKFKKD
VTNAWKDINK EFFRPTEVPM FVLERVLNLT RAADTLYKEK DAYTNAKGKL KNMINSILIE
SVKI
