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Bicyclo-germacrene synthase (EC 4.2.3.100) (Allo-aromadendrene synthase) (EC 4.2.3.-) (Geraniol synthase) (EC 3.1.7.11) (Limonene synthase) (EC 4.2.3.20) (Terpene synthase 4) (OvTPS4) (Terpinolene synthase) (EC 4.2.3.113)

 BCGS_ORIVU              Reviewed;         555 AA.
E2E2N7;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 1.
25-MAY-2022, entry version 33.
RecName: Full=Bicyclo-germacrene synthase {ECO:0000305|PubMed:20419468};
EC=4.2.3.100 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
AltName: Full=Allo-aromadendrene synthase {ECO:0000305|PubMed:20419468};
EC=4.2.3.- {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
AltName: Full=Geraniol synthase {ECO:0000305|PubMed:20419468};
EC=3.1.7.11 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
AltName: Full=Limonene synthase {ECO:0000305|PubMed:20419468};
EC=4.2.3.20 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
AltName: Full=Terpene synthase 4 {ECO:0000303|PubMed:20419468};
Short=OvTPS4 {ECO:0000303|PubMed:20419468};
AltName: Full=Terpinolene synthase {ECO:0000305|PubMed:20419468};
EC=4.2.3.113 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
Name=TPS4;
Origanum vulgare (Wild marjoram).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Origanum.
NCBI_TaxID=39352;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE
SPECIFICITY, AND PATHWAY.
STRAIN=cv. f02-04; TISSUE=Trichome gland;
PubMed=20419468; DOI=10.1007/s11103-010-9636-1;
Crocoll C., Asbach J., Novak J., Gershenzon J., Degenhardt J.;
"Terpene synthases of oregano (Origanum vulgare L.) and their roles in the
pathway and regulation of terpene biosynthesis.";
Plant Mol. Biol. 73:587-603(2010).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
Crocoll C.;
"Biosynthesis of the phenolic monoterpenes, thymol and carvacrol, by
terpene synthases and cytochrome P450s in oregano and thyme.";
Thesis (2011), Friedrich Schiller University of Jena, Germany.
[3]
TISSUE SPECIFICITY.
DOI=10.1016/j.indcrop.2018.07.006;
Jan S., Mir J.I., Shafi W., Faktoo S.Z., Singh D.B., Wijaya L.,
Alyemeni M.N., Ahmad P.;
"Divergence in tissue-specific expression patterns of genes associated with
the terpenoid biosynthesis in two oregano species Origanum vulgare L., and
Origanum majorana.";
Ind. Crops Prod. 123:546-555(2018).
-!- FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes
natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-
farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene.
The product formation is dependent on the metal ions present and in
presence of manganese, bicyclo-germacrene is greatly favored while both
alloaromadendrene and bicyclo-germacrene are produced in equivalent
amounts in the presence of magnesium. Can also convert geranyl
diphosphate (GPP) to terpinolene, limonene and geraniol, and this
conversion is not affected by the presence of magnesium or manganese.
{ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}.
-!- CATALYTIC ACTIVITY:
Reaction=(2E,6E)-farnesyl diphosphate = bicyclogermacrene +
diphosphate; Xref=Rhea:RHEA:31999, ChEBI:CHEBI:33019,
ChEBI:CHEBI:63709, ChEBI:CHEBI:175763; EC=4.2.3.100;
Evidence={ECO:0000269|PubMed:20419468};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32000;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
-!- CATALYTIC ACTIVITY:
Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
ChEBI:CHEBI:58057; EC=4.2.3.113;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
-!- CATALYTIC ACTIVITY:
Reaction=(2E)-geranyl diphosphate = (4R)-limonene + diphosphate;
Xref=Rhea:RHEA:10940, ChEBI:CHEBI:15382, ChEBI:CHEBI:33019,
ChEBI:CHEBI:58057; EC=4.2.3.20;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10941;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
-!- CATALYTIC ACTIVITY:
Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate;
Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
-!- CATALYTIC ACTIVITY:
Reaction=(2E,6E)-farnesyl diphosphate = allo-aromadendrene +
diphosphate; Xref=Rhea:RHEA:67400, ChEBI:CHEBI:33019,
ChEBI:CHEBI:166670, ChEBI:CHEBI:175763;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67401;
Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:20419468};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:20419468};
Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
{ECO:0000250|UniProtKB:E2E2P0};
-!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
{ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0M3Q1Q3}.
-!- TISSUE SPECIFICITY: Expressed in peltate glandular trichomes
(PubMed:20419468). Present at low levels in flowers, leaves and stems
(Ref.3). {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.3}.
-!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
the catalytic activity, presumably through binding to Mg(2+).
{ECO:0000250|UniProtKB:Q9X839}.
-!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; GU385973; ADK73618.1; -; mRNA.
AlphaFoldDB; E2E2N7; -.
SMR; E2E2N7; -.
KEGG; ag:ADK73618; -.
UniPathway; UPA00213; -.
GO; GO:0034002; F:(R)-limonene synthase activity; IEA:RHEA.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
CDD; cd00684; Terpene_cyclase_plant_C1; 1.
Gene3D; 1.10.600.10; -; 1.
Gene3D; 1.50.10.130; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR034741; Terpene_cyclase-like_1_C.
InterPro; IPR044814; Terpene_cyclase_plant_C1.
InterPro; IPR001906; Terpene_synth_N.
InterPro; IPR036965; Terpene_synth_N_sf.
InterPro; IPR005630; Terpene_synthase_metal-bd.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF01397; Terpene_synth; 1.
Pfam; PF03936; Terpene_synth_C; 1.
SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF48576; SSF48576; 1.
1: Evidence at protein level;
Hydrolase; Lyase; Magnesium; Manganese; Metal-binding.
CHAIN 1..555
/note="Bicyclo-germacrene synthase"
/id="PRO_0000418650"
REGION 316..322
/note="Homodimerization"
/evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
REGION 392..429
/note="Homodimerization"
/evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
MOTIF 311..315
/note="DDXXD motif"
/evidence="ECO:0000250|UniProtKB:Q9X839"
METAL 311
/note="Magnesium 1"
/evidence="ECO:0000250|UniProtKB:Q40577"
METAL 311
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:Q40577"
METAL 315
/note="Magnesium 1"
/evidence="ECO:0000250|UniProtKB:Q40577"
METAL 315
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:Q40577"
METAL 459
/note="Magnesium 3"
/evidence="ECO:0000250|UniProtKB:Q40577"
METAL 467
/note="Magnesium 3"
/evidence="ECO:0000250|UniProtKB:Q40577"
SEQUENCE 555 AA; 64443 MW; 6BDB5899A7C55A43 CRC64;
MEIYSPVVPA VKDVKRLDEI RKSAKFHPSI WGDFFLSYNS DNTQISEAEE EEVAKQKEAV
RELLAQVPEG STYKMELIDL IQRLGVNYHF EKEIHDSLNY IHENSQHNDD EVRTTALRFR
LLRQQGYRVP CDVFRKFTDG EGNFATALTN DVEGLLELYE ASHLATRGEE ILDRAMEFSS
SHLQALLNQH LVGSVSLSKR VDEALKMPIR KTLTRLGARK FISLYQEDES RNELLLNFAK
LDFNMVQKMH QRELSDATRW WKKLEVAKRM PYARDRVVEC FFWIVGVYFE PCYATARRIL
SKAINMASIV DDTYEYATLD ELQILTDAIQ RWDVNETLED SPPHVQMCYK ALIQAYAEIE
DEVVENFGGE ELYRVQYAIE HVKQSAVAFF EEAKWIYNNS IPTVEEYMKV AFVTCGYMML
STTSLVGVGS DRVSKADFDW IVNEPLIVRA SCVICRLMDD LVGDEYEEKP SSVLCYMKQY
VVSKDEARAR LEQQVKDAWK DMNEECIEPR PASMQILTRV LNLGRVIHLL YREGDSYTDP
NRSKEWVKMV FVDPI


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