TER_NICAL
ID TER_NICAL Reviewed; 543 AA.
AC H6WZF2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 35.
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=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;
GN Name=TER {ECO:0000303|PubMed:21527560};
OS Nicotiana alata (Winged tobacco) (Persian 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=4087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=cv. TW 7;
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 and 1,8-cineole
CC (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 -!- 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; JQ346173; AFB82540.1; -; mRNA.
DR BRENDA; 4.2.3.108; 7435.
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:0080015; F:sabinene synthase activity; 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 ?..543
FT /note="Terpineol synthase, chloroplastic"
FT /id="PRO_0000455076"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 300..304
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:H2ELN1"
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 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 543 AA; 63682 MW; 8E094547159439C0 CRC64;
MNTEPSPNHY SAISSSDQNL TRRSGNYQPT MWDFEYIQSI HNDYAGDKYM KRFNELKEEM
KKMIMAEGSQ ELEKLELIDN LQRLGVSYHF KHEIMQILSS IKQHSTPADS LYATALKFRL
LREHGFHISQ EIFDGLSETH TKDTKGMLYL YEASFLATEG ESELEQAWTE KHLREYLKNK
NIDQNVAKLV HRALELPLHW RMLRLEARWF ISFYKKRQDM IPLLLELAIL DFNIVQAAHI
QDLKYVARWW KETGLAENLP FARDRLVENF FWTIGVNFLP QYGYFRRIET KVNALVTTID
DVYDVFGTLD ELQCFTDAIQ RWNTDELDNL PDNMKMCYFA LDDFINEVAC DALIVPYLRN
AWTDLCKSYL IEAKWYFSKY IPTMEEYMDN AWISISAPVI LVHAYFLIAN PVNKEALHYL
RNYHDIIRWS ALILRLANDL GTSSDELKRG DVPKSIQCYM NEKKVSEEEA RQHIRLLISE
TWKKLNEAHN VAAHPFPKMF VKSAMNLARM AQCMYQHGDG HGGQNSETQN RIMALLFESI
PPA
