GERDS_LAVAN
ID GERDS_LAVAN Reviewed; 549 AA.
AC U3LVL5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Germacrene D synthase {ECO:0000303|PubMed:24078339};
DE Short=LaGERDS {ECO:0000303|PubMed:24078339};
DE EC=4.2.3.75 {ECO:0000269|PubMed:24078339};
DE AltName: Full=(-)-germacrene D synthase {ECO:0000305};
DE AltName: Full=Bicyclogermacrene synthase {ECO:0000305};
DE EC=4.2.3.100 {ECO:0000269|PubMed:24078339};
GN Name=GERDS {ECO:0000303|PubMed:24078339};
OS Lavandula angustifolia (Lavender).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC Lavandula.
OX NCBI_TaxID=39329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24078339; DOI=10.1007/s11103-013-0131-3;
RA Jullien F., Moja S., Bony A., Legrand S., Petit C., Benabdelkader T.,
RA Poirot K., Fiorucci S., Guitton Y., Nicole F., Baudino S., Magnard J.L.;
RT "Isolation and functional characterization of a tau-cadinol synthase, a new
RT sesquiterpene synthase from Lavandula angustifolia.";
RL Plant Mol. Biol. 84:227-241(2014).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC sesquiterpenes and sesquiterpenoid alcohols (PubMed:24078339). Converts
CC farnesyl diphosphate (FPP) to germacrene D (PubMed:24078339). Converts
CC FPP to bicyclogermacrene (PubMed:24078339). Germacrene D is the major
CC product (PubMed:24078339). {ECO:0000269|PubMed:24078339}.
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:24078339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12017;
CC Evidence={ECO:0000269|PubMed:24078339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = bicyclogermacrene +
CC diphosphate; Xref=Rhea:RHEA:31999, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:63709, ChEBI:CHEBI:175763; EC=4.2.3.100;
CC Evidence={ECO:0000269|PubMed:24078339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32000;
CC Evidence={ECO:0000269|PubMed:24078339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JX401284; AGL98420.1; -; mRNA.
DR AlphaFoldDB; U3LVL5; -.
DR SMR; U3LVL5; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0052577; F:germacrene-D synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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 Lyase; Magnesium; Metal-binding.
FT CHAIN 1..549
FT /note="Germacrene D synthase"
FT /id="PRO_0000452463"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:U3LW50"
FT BINDING 271
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 448
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 451
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 549 AA; 63973 MW; B6C5DBA68C50B389 CRC64;
MEIHSSVVPA ITNVKSLDEI RRSAKFHPTV WGDYFLAYNS DNTEITAAEH EEHAKQKEMV
KKLLTLAPND PTDKMQLIDA IQRLGLQYHF EKEIQEILQS IHANFKADKD LHTVALRFRL
LRQHGYNVAC DVFNNFLNKE GDFMESITND FEGLLSLYEA AYLGTHGEEI LDKAIEFCSF
HLQSSLPQIS NVSLSKRVEE ALYIPTHKSL TRFGARKFIP IYEEDESHKK VLLNLAKLDF
NIVQKIHQKE LSDLTRWWTK LEVPKNMPYS RDRLVELFFW IVGVYFEPQF TTARRILVKA
ISMASLIDDT YEHATLDELK VLTDVIERWD TNAVIKDWPP YTQMCYKYLF DTYAEIEDEV
EERESYRVQY AKKEMQKLVR AYFDEAKWLY KNYLPTWEEY MKVSTVTGAY MMLSTTSLVG
MGDLVTKQDF DWVVREPLIV RASSVISRLM DDLVGDEDEQ KPSGALCYMK QYGVSKEEAC
AEVRKHVKNA WKDMNQECLE PRPASMQVLT RVVNLGRVIN LLYTGDDWYG NPLGSKEWVK
MVFVEPLTI
