GCDS_ORIVU
ID GCDS_ORIVU Reviewed; 563 AA.
AC E2E2N8;
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=(-)-germacrene D synthase {ECO:0000303|PubMed:20419468};
DE EC=4.2.3.75 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE AltName: Full=Terpene synthase 3 {ECO:0000303|PubMed:20419468};
DE Short=OvTPS3 {ECO:0000303|PubMed:20419468};
GN Name=TPS3 {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 sesquiterpenes
CC natural products (Ref.2). Sesquiterpene synthase that catalyzes mainly
CC the formation of (-)-germacrene D and minor amounts of other
CC sesquiterpenes (e.g. bicyclo-germacrene) from farnesyl diphosphate
CC (FPP) (PubMed:20419468, Ref.2). Triggers also moderate amounts
CC formation of myrcene, limonene, terpinolene and linalool in the
CC presence of geranyl diphosphate (GPP) (PubMed:20419468, Ref.2).
CC {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate;
CC Xref=Rhea:RHEA:12016, ChEBI:CHEBI:33019, ChEBI:CHEBI:49044,
CC ChEBI:CHEBI:175763; EC=4.2.3.75;
CC Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12017;
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 -!- 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; GU385976; ADK73619.1; -; mRNA.
DR SMR; E2E2N8; -.
DR UniPathway; UPA00213; -.
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 Coiled coil; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..563
FT /note="(-)-germacrene D synthase"
FT /id="PRO_0000453318"
FT REGION 320..326
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT REGION 392..429
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT COILED 44..71
FT /evidence="ECO:0000255"
FT MOTIF 314..318
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9X839"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 318
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 318
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 459
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 467
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ SEQUENCE 563 AA; 65463 MW; F3C0BECC10745BBE CRC64;
MAEICASAAP ISTKNTSVEE LRRSVTYHPS VWRDHFLSYT NDVTEITAAE KEELEKQKEK
VKNLLDQTPN DSTLKIELID AIQRLGFGYH FEEVIDESLG EVYDRYEMPS GKDDEDEIRV
RSLRFRLLRQ QGYRVPCDVF EKLLDDKGNF KDSLITDVEG LLSLYEASNY GINGEEIMDK
ALKFSSSHLE GSIHKMPTSL SRRVKEALDM PISKTLTRLG ARKFISLYQE DESHNELLLK
FAKLDFNIVQ KMHQRELHHI TRWWEGLEFG KKLPFARDRV VECFFWILGV YFEPKYEIAR
RFLTKVISMT SILDDIYDVY GSLDELRRLT HAIQRWDISV GDELPPYMRI CYEALLGVYS
EMEDEMAKKG QSYRLLYARQ EMIKLVMAYM VEAEWCFSKY FPTMEEYMKQ ALVSGAYMML
STTSLVGMED LNITKHDFDW ITSEPPMLRA ASVICRLMDD MVGHGIEQKI ISVDCYMREN
GCSKEEACRE FWNRVKKAWK CMNEECLEPR AASMAILARV LNLARVINLL YVGEDAYGSS
STKTKNFIKS VLVDPIHSIE YHI
