TER_NICLA
ID TER_NICLA Reviewed; 522 AA.
AC H2ELN1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Terpineol synthase, chloroplastic {ECO:0000303|PubMed:21527560};
DE EC=4.2.3.111 {ECO:0000269|PubMed:21527560};
DE AltName: Full=1,8-cineol synthase, chloroplastic {ECO:0000303|PubMed:21527560};
DE EC=4.2.3.108 {ECO:0000269|PubMed:21527560};
DE AltName: Full=Alpha-pinene synthase {ECO:0000303|PubMed:21527560};
DE EC=4.2.3.- {ECO:0000269|PubMed:21527560};
DE AltName: Full=Beta-myrcene synthase {ECO:0000303|PubMed:21527560};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21527560};
DE AltName: Full=Limonene synthase {ECO:0000303|PubMed:21527560};
DE EC=4.2.3.- {ECO:0000269|PubMed:21527560};
DE AltName: Full=Sabinene synthase {ECO:0000303|PubMed:21527560};
DE EC=4.2.3.- {ECO:0000269|PubMed:21527560};
DE Flags: Precursor; Fragment;
GN Name=TER {ECO:0000303|PubMed:21527560};
OS Nicotiana langsdorffii (Langsdorff's tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=118700;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. TW 74;
RX PubMed=21527560; DOI=10.1093/mp/ssr021;
RA Faehnrich A., Krause K., Piechulla B.;
RT "Product variability of the 'cineole cassette' monoterpene synthases of
RT related Nicotiana species.";
RL Mol. Plant 4:965-984(2011).
CC -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC monoterpene natural products of the 'cineole cassette', volatile
CC compounds present in floral scent (PubMed:21527560). Catalyzes the
CC conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and,
CC as minor products, sabinene, beta-myrcene, limonene, alpha-pinene and
CC 1,8-cineole (PubMed:21527560). {ECO:0000269|PubMed:21527560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC EC=4.2.3.111; Evidence={ECO:0000269|PubMed:21527560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552;
CC Evidence={ECO:0000269|PubMed:21527560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene;
CC Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637;
CC Evidence={ECO:0000269|PubMed:21527560};
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:21527560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:21527560};
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:21527560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641;
CC Evidence={ECO:0000269|PubMed:21527560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate;
CC Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108;
CC Evidence={ECO:0000269|PubMed:21527560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32544;
CC Evidence={ECO:0000269|PubMed:21527560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21527560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC Evidence={ECO:0000269|PubMed:21527560};
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:21527560}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to flowers. {ECO:0000269|PubMed:21527560}.
CC -!- DEVELOPMENTAL STAGE: In flowers, present in pistils and in the adaxial
CC and abaxial epidermis of the petals (PubMed:21527560). Maximal enzyme
CC activities are reached at the second day after anthesis when flowers
CC are fully opened (PubMed:21527560). {ECO:0000269|PubMed:21527560}.
CC -!- INDUCTION: Enzyme activity levels follow a circadian oscillation,
CC reaching a maxima at the transition from day to night (diurnal rhythm).
CC {ECO:0000269|PubMed:21527560}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; JN989317; AEX09186.1; -; mRNA.
DR BRENDA; 4.2.3.108; 3637.
DR BRENDA; 4.2.3.111; 3637.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102313; F:1,8-cineole synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IDA:UniProtKB.
DR GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0080015; F:sabinene synthase activity; IDA:UniProtKB.
DR GO; GO:0046248; P:alpha-pinene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046250; P:limonene biosynthetic process; IDA:UniProtKB.
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 Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT <1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..522
FT /note="Terpineol synthase, chloroplastic"
FT /id="PRO_0000455075"
FT MOTIF 279..283
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 421
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AEX09186.1"
SQ SEQUENCE 522 AA; 61316 MW; 7BF291A6F6F0E8C1 CRC64;
RRSGNYQPTM WDFEYIQSIH NDYAGDKYMK RFNELKEEMK KMIMAEGSQE LEKLELIDNL
QRLGVSYHFK HEIMQILSSI KQHSTPADSL YATALKFRLL REHGFHISQE IFDGLSETHT
KDTKGMLYLY EASFLATEGE SELEQAWTEK HLREYLKNKN IDQNVAKLVH RALELPLHWR
MLRLEARWFI SFYKKRQDMI PLLLELAILD FNIVQAAHIQ DLKYVARWWK ETGLAENLPF
ARDRLVENFF WTIGVNFLPQ YGYSRRIETK VNALVTAIDD VYDVFGTLDE LQCFTDAIQR
WNTDELDNLP DNMKMCYFAL DDFINEVACD ALIVPYLRNA WTDLCKSYLI EAKWYFSKYI
PTMEEYMDNA WISISAPVIL VHAYFLIANP VNKEALHYLR NYHDIIRWSA LILRLANDLG
TSSDELKRGD VPKSIQCYMN EKKVSEEEAR QHIRLLISET WKKLNEAHNV AAHPFPKMFV
KSAMNLARMA QCMYQHGDGH GGQNSETQNR IMALLFESIP PA
