TPS1F_ORIVU
ID TPS1F_ORIVU Reviewed; 601 AA.
AC E2E2P1;
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. f02-04; 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, leaves and stems
CC (Ref.3). {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; GU385979; ADK73622.1; -; mRNA.
DR SMR; E2E2P1; -.
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_0000453314"
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; 69767 MW; 42BB66CFFE65D6AF CRC64;
MSTISIHHVG ILRNPLPSKN KRALINNPWS LSLPRSSSAS RLVKPCRISS KPDTKPAEIT
RRSANYEPSL WDFDYLQSLN GHQHYKKEEQ LKREEELIVQ VKMLLGTKME AVKQLELIDD
LKNLGLSYFF RDEIKKILTS IYNNSFENNN KVGDLYFTAL GFRLLRQHGF NVSQRIFDCF
KNEKGIHFDE TLIGEDIKAT LQLYEASFHL REGENTLELA RQISTKYLQK MVDEGRINDE
NLSSWIRHSL DLPLHWRIQR LEARWFLDAY AAREDKNPLI FELAKLDFNI IQATQQEELK
EVSRWWNDSC LAEKLPFVRD RIVKCCFWAV GLFELLEFGY QRKITAIIIH LITAIDDVYD
VYGTLDELQL LTNAIRRWDT LSIDQLPYYM QLCYMTLHNY VSDLGYDILK DRGINTIPHI
HQTWVSLVEA YLKEAKWYES GYTPSLEEYL NNAGFSIGVI PIVVALELSI PNSTIHHRTR
IDHRHEILHQ SGLVLRLADD LGTAQHEMEK GDVPKAIQCY MKDTNASEEE AREHVRFMIG
EAWKGLNTAM AKADDCPFTE QAVEAAANLG RAAQFIYLDG DGHGNFQIRQ HVEKLFFHPY
V
