TPS12_SOLHA
ID TPS12_SOLHA Reviewed; 545 AA.
AC G8H5M8;
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=Sesquiterpene synthase 12 {ECO:0000303|PubMed:21818683};
DE Short=ShTPS12 {ECO:0000303|PubMed:21818683};
DE AltName: Full=(E)-beta-ocimene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.106 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(Z)-gamma-bisabolene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Alpha-humulene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.104 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta bisabolene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta caryophyllene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.57 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-myrcene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Gamma-curcumene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Limonene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Terpinolene synthase TPS12 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.113 {ECO:0000269|PubMed:21818683};
GN Name=TPS12 {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,8E)-alpha-humulene and
CC (-)-(E)-beta-caryophyllene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-
CC FPP) into beta-bisabolene, gamma-curcumene and (Z)-gamma-bisabolene
CC (PubMed:21818683). Can act with a low efficiency as a monoterpene
CC synthase with geranyl diphosphate (GPP) as substrate, thus producing
CC beta-myrcene, (E)-beta-ocimene, limonene and terpinolene
CC (PubMed:21818683). {ECO:0000269|PubMed:21818683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.104;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
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)-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=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64280; EC=4.2.3.106;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:68788, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49238, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68789;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = diphosphate + gamma-curcumene;
CC Xref=Rhea:RHEA:68784, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374,
CC ChEBI:CHEBI:63696; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68785;
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; JN402389; AEM23826.1; -; mRNA.
DR SMR; G8H5M8; -.
DR BRENDA; 4.2.3.104; 3102.
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..545
FT /note="Sesquiterpene synthase 12"
FT /id="PRO_0000454683"
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 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 545 AA; 63985 MW; 80CB9C76012223A2 CRC64;
MAASSADKSR PLANFSPTVW GYHFLSYTPE ISSQEKHEVD ELKEIFRKML VETCDNSTQK
LVLIDTIQRL GVAYHFDNEI ETSIQNIFDA SKQNDNDDNL HIVSLRFRLV RQQGHYMSSD
VFKQFTNQDG KFKETLTNDV QGLLSLYEAS HLRVRDEEIL EEALTFTTTH LESIVSNLSN
NNKVEVSEAL TQPIRMTLPR MGARKYISIY ENNDAHNHLL LKFAKLDFNM LQKLHQRELS
DLTRWWKDLD FANKYPYARD RLVECYFWIL GVYFEPKYSR ARKMMTKVIQ MASFFDDTFD
AYATFDELEP FNDAIQRWDI NAIDSVPPYL RHAYQALLDI YSEMEQELAK EFKSDRVYYA
KYEMKKLVRA YFKEAQWLND DNHIPKYEEH MENAMVSAGY MMGATTCLVG VDEFISQETF
EWIINEPLIV RASSLIARAM DDIAGHEVEQ QREHGASLIE CYMKDYGVSK QEAYVKFQKE
VTNGWMDINK EFFCLDVQVP KFVLERVLNF TRVINTLYKE KDEYTNSKGK FKNMIITLLV
ESVEI
