BOMS_ORIVU
ID BOMS_ORIVU Reviewed; 595 AA.
AC E2E2N3;
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=(E)-beta-ocimene synthase, chloroplastic {ECO:0000303|PubMed:20419468};
DE EC=4.2.3.106 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE AltName: Full=Terpene synthase 7 {ECO:0000303|PubMed:20419468};
DE Short=OvTPS7 {ECO:0000303|PubMed:20419468};
DE Flags: Precursor;
GN Name=TPS7 {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 monoterpenes natural products
CC (Ref.2). Monoterpene synthase that catalyzes mainly the formation of
CC (E)-beta-ocimene and minor amounts of other monoterpenes (e.g. myrcene,
CC (Z)-beta-ocimene, alpha- and gamma-terpinene) from geranyl diphosphate
CC (GPP) (PubMed:20419468, Ref.2). {ECO:0000269|PubMed:20419468,
CC ECO:0000269|Ref.2}.
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:20419468, ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
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 in flowers, leaves 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; GU385967; ADK73614.1; -; mRNA.
DR SMR; E2E2N3; -.
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..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..595
FT /note="(E)-beta-ocimene synthase, chloroplastic"
FT /id="PRO_0000453321"
FT REGION 356..362
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT REGION 428..465
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT MOTIF 350..354
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9X839"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 501
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ SEQUENCE 595 AA; 69381 MW; 8BDB2D0DC6D597E4 CRC64;
MSTISINLMS IIRNPLHSKS KRALINKHPS SSASRLVQPC RISSKIDTKP AEITRRSGNY
EPSLWDFDYL QSLNTHHHYK KEEQLKREEE LIVQVKMLLG TKMEAVEQLE LIDDLKNLGL
SYFFRDEIKK ILTSIYNNSF ENNNKVGDLY FTALGFRLLR QHGFNVSQRI FDCFKNEKGS
HFDETLIGED IKATLQLYEA SFHLREGENT LELARQISTK YLQKMVDEGR INDENLSSWI
RHSLDLPLHW RIQRLEARWF LDAYAVREDK NPLIFELAKL DFNIIQATQQ EELKEVSRWW
NDSCLAEKLP FLRDRIVEAY FWGVALFELL EFGYQRKITA IIIILVTAID DVYDVYGTLD
ELQLFTDVIR RWNTQSIDQL PYYMQLCYMT LYNYVSNLGY EILKDRGINT IPHIHQSWVS
LVEAFLKEEE WYESGYTPSL KEYLNNASIS VGAIAVVIAL ELSIPNSTIH HRTRIDHRHK
ILHLSGLVSR LANDLGTAQH EMEKGNVPTA IQCYMKDTNA SEEEAWEHVR FMIGEAWKRL
NTAMAEADDC PFTEQAVEAA ANFGRAAQFI YREGDGHGHF QIHQHVENLF FHPYV
