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TPS1D_ORIVU
ID   TPS1D_ORIVU             Reviewed;         601 AA.
AC   E2E2P2;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Beta-phellandrene synthase {ECO:0000303|PubMed:20419468};
DE            EC=4.2.3.- {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE   AltName: Full=Sabinene synthase {ECO:0000303|PubMed:20419468};
DE            EC=4.2.3.110 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE   AltName: Full=Terpene synthase 1, chloroplastic {ECO:0000303|PubMed:20419468};
DE            Short=OvTPS1 {ECO:0000303|PubMed:20419468};
DE   Flags: Precursor;
GN   Name=TPS1 {ECO:0000303|PubMed:20419468};
OS   Origanum vulgare (Wild marjoram).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Origanum.
OX   NCBI_TaxID=39352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. d06-01; TISSUE=Trichome gland;
RX   PubMed=20419468; DOI=10.1007/s11103-010-9636-1;
RA   Crocoll C., Asbach J., Novak J., Gershenzon J., Degenhardt J.;
RT   "Terpene synthases of oregano (Origanum vulgare L.) and their roles in the
RT   pathway and regulation of terpene biosynthesis.";
RL   Plant Mol. Biol. 73:587-603(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RA   Crocoll C.;
RT   "Biosynthesis of the phenolic monoterpenes, thymol and carvacrol, by
RT   terpene synthases and cytochrome P450s in oregano and thyme.";
RL   Thesis (2011), Friedrich Schiller University of Jena, Germany.
RN   [3]
RP   TISSUE SPECIFICITY.
RX   DOI=10.1016/j.indcrop.2018.07.006;
RA   Jan S., Mir J.I., Shafi W., Faktoo S.Z., Singh D.B., Wijaya L.,
RA   Alyemeni M.N., Ahmad P.;
RT   "Divergence in tissue-specific expression patterns of genes associated with
RT   the terpenoid biosynthesis in two oregano species Origanum vulgare L., and
RT   Origanum majorana.";
RL   Ind. Crops Prod. 123:546-555(2018).
CC   -!- FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural
CC       products (PubMed:20419468, Ref.2). Monoterpene synthase that catalyzes
CC       mainly the formation of olefins such as sabinene and beta-phellandrene,
CC       and minor amounts of other monoterpenes (e.g. myrcene, gamma-terpinene,
CC       alpha-thujene and alpha-pinene) from geranyl diphosphate (GPP)
CC       (PubMed:20419468, Ref.2). {ECO:0000269|PubMed:20419468,
CC       ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = beta-phellandrene + diphosphate;
CC         Xref=Rhea:RHEA:25504, ChEBI:CHEBI:33019, ChEBI:CHEBI:48741,
CC         ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:20419468,
CC         ECO:0000269|Ref.2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25505;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (1R,5R)-sabinene + diphosphate;
CC         Xref=Rhea:RHEA:32547, ChEBI:CHEBI:33019, ChEBI:CHEBI:50029,
CC         ChEBI:CHEBI:58057; EC=4.2.3.110;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32548;
CC         Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:E2E2P0};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:E2E2P0};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:E2E2P0};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0M3Q1Q3}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in peltate glandular trichomes
CC       (PubMed:20419468). Present at low levels in flowers and stems (Ref.3).
CC       {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.3}.
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:Q9X839}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; GU385980; ADK73623.1; -; mRNA.
DR   SMR; E2E2P2; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Manganese; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..601
FT                   /note="Beta-phellandrene synthase"
FT                   /id="PRO_0000453315"
FT   REGION          362..368
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT   REGION          434..471
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT   MOTIF           356..360
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X839"
FT   BINDING         356
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         356
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         360
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         360
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         499
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         507
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ   SEQUENCE   601 AA;  69639 MW;  1CFD87693124220D CRC64;
     MSTISIHHVG ILRNPLPSKN KRALINNPWS LSLPRSSSAS RLVKPCRISS KTDTNPAEIT
     RRSANYEPSL WDFDYIQSLN GHQHYKKEKQ LKREEELIVQ VKMLLGTKME AVKQLELIDD
     LKNLGLSYFF RDEIKKILTS IYNNSFENNN QVGDLYFTAL GFRLLRQHGF NVSQRIFDCF
     KNEKGSHFDE TLIGEDIKAT LQLYETSFHL REGENTLELA RQISTKYLQK MVDEGRINDE
     NLSSWIRHSL DLPLHWRIQR LEARWSLDAY AAREDKNPLI FELAKLDFNI IQATQQEELK
     EVSRWWNDSC LAEKLPFVRD RVVECYFWAV GLFDCHDYGF QRKITAAVNI LITAIDDVYD
     VYGTLDELQL FTDVIRRWDT QSIDQLPYYM QLCYLMLYNF VSSLGYDILK DRGINTILHL
     HQSWVSVVEA YLKEAEWYES GYAPSLEEYL SIATISIGLI PIVIPLDLSI PNSTIHRHTR
     IDHRHEILNL SGMVLRLADD LGTASSELER GDVPKAIQCY MKDTNASEEE AREHVRFLIG
     EAWKELNTAM AEPDDHPFTE QGAGAAANIG RAAQFIYLEG DGHAHFQNHQ HLENLFFHPY
     V
 
 
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