TPS12_SOLLC
ID TPS12_SOLLC Reviewed; 548 AA.
AC D5KXD2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Sesquiterpene synthase 12 {ECO:0000303|PubMed:21813655};
DE Short=SlTPS12 {ECO:0000303|PubMed:21813655};
DE Short=Terpene synthase 12 {ECO:0000303|PubMed:21813655};
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:20431087, ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE EC=4.2.3.104 {ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, 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:20431087, ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE EC=4.2.3.57 {ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655, 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:21813655};
GN Synonyms=CAHS {ECO:0000312|EMBL:ADD96698.1};
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 [MRNA].
RC STRAIN=cv. M82; TISSUE=Trichome gland;
RX PubMed=20431087; DOI=10.1104/pp.110.157214;
RA Schilmiller A.L., Miner D.P., Larson M., McDowell E., Gang D.R.,
RA Wilkerson C., Last R.L.;
RT "Studies of a biochemical factory: tomato trichome deep expressed sequence
RT tag sequencing and proteomics.";
RL Plant Physiol. 153:1212-1223(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND GENE FAMILY.
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:21813655, PubMed:20431087, PubMed:21818683).
CC Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into
CC (1E,4E,8E)-alpha-humulene and (-)-(E)-beta-caryophyllene, and of
CC (2Z,6Z)-farnesyl diphosphate ((ZZ)-FPP) into beta-bisabolene, gamma-
CC curcumene and (Z)-gamma-bisabolene (PubMed:21813655, PubMed:20431087,
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:20431087,
CC ECO:0000269|PubMed:21813655, 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:20431087, ECO:0000269|PubMed:21813655,
CC ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
CC Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655,
CC 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:20431087, ECO:0000269|PubMed:21813655,
CC ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:20431087, ECO:0000269|PubMed:21813655,
CC 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 = 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 -!- 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 -!- 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:20431087, ECO:0000269|PubMed:21813655,
CC ECO:0000269|PubMed:21818683}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, to a lower extent in
CC stems, trichomes, flowers and roots and, at low levels, in fruits.
CC {ECO:0000269|PubMed:21813655, 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; GU647162; ADD96698.1; -; mRNA.
DR EMBL; JN412092; AEP82783.1; -; Genomic_DNA.
DR RefSeq; NP_001234766.1; NM_001247837.1.
DR SMR; D5KXD2; -.
DR GeneID; 104648118; -.
DR BioCyc; MetaCyc:MON-16135; -.
DR BRENDA; 4.2.3.104; 3101.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; D5KXD2; baseline.
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..548
FT /note="Sesquiterpene synthase 12"
FT /id="PRO_0000454690"
FT MOTIF 299..303
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 548 AA; 64321 MW; 6ED001507BC178D4 CRC64;
MASSSANKCR PLANFHPTVW GYHFLSYTHE ITNQEKVEVD EYKETIRKML VEAPEGSEQK
LVLIDAMQRL GVAYHFDNEI ETSIQNIFDA SSKQNDNDNN LYVVSLRFRL VRQQGHYMSS
DVFKQFINQD GKFKETLTND VQGLLSLYEA SHLRVRDEEI LEEALTFTTT HLESTVSNLS
NNNSLKAEVT EAFSQPIRMT LPRVGARKYI SIYENNDAHN HLLLKFAKLD FNMLQKLHQR
ELSDLTRWWK DLDFANKYPY ARDRLVECYF WILGVYFEPK YSRARKMMTK VIQMASFFDD
TFDAYATFDE LEPFNNAIQR WDINAIDSVP PYLRHAYQAL LDIYSEMEQA LAKEFKSDRV
YYAKYEMKKL VRAYFKEAQW LNNDNHIPKY EEHMENAMVS AGYMMGATTC LVGVEEFISK
ETFEWMINEP LIVRASSLIA RAMDDIVGHE VEQQREHGAS LIECYMKDYG VSKQEAYVKF
QKEVTNGWMD INREFFCPDV EVPKFVLERV LNFTRVINTL YKEKDEYTNS KGKFKNMIIS
LLVESVEI
