GEAS_LAVPL
ID GEAS_LAVPL Reviewed; 547 AA.
AC T1RRI5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Germacrene A synthase {ECO:0000303|PubMed:24943828};
DE Short=LpGEAS {ECO:0000303|PubMed:24943828};
DE EC=4.2.3.- {ECO:0000269|PubMed:24943828};
DE AltName: Full=Beta-elemene synthase {ECO:0000303|PubMed:24943828};
DE EC=4.2.3.- {ECO:0000269|PubMed:24943828};
GN Name=GEAS {ECO:0000303|PubMed:24943828};
OS Lavandula pedunculata subsp. lusitanica (French 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=1343917;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=24943828; DOI=10.1111/ppl.12241;
RA Benabdelkader T., Guitton Y., Pasquier B., Magnard J.L., Jullien F.,
RA Kameli A., Legendre L.;
RT "Functional characterization of terpene synthases and chemotypic variation
RT in three lavender species of section Stoechas.";
RL Physiol. Plantarum 153:43-57(2015).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds widely used in aromatherapy and folk medicine, and
CC present in culinary herbs (PubMed:24943828). Mediates the conversion of
CC (2E,6E)-farnesyl diphosphate (FPP) into germacrene A and beta-elemene
CC (PubMed:24943828). Not able to use (2E)-geranyl diphosphate (GPP) as
CC substrate (PubMed:24943828). {ECO:0000269|PubMed:24943828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene A;
CC Xref=Rhea:RHEA:25452, ChEBI:CHEBI:33019, ChEBI:CHEBI:36517,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:24943828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25453;
CC Evidence={ECO:0000269|PubMed:24943828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,2S,4R)-beta-elemene +
CC diphosphate; Xref=Rhea:RHEA:68712, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62855, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:24943828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68713;
CC Evidence={ECO:0000269|PubMed:24943828};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:24943828}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:24943828}.
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:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JX501513; AGN72800.1; -; mRNA.
DR BRENDA; 4.2.3.23; 13954.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102889; F:beta-elemene synthase activity; IDA:UniProtKB.
DR GO; GO:0034005; F:germacrene-A synthase activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
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 Chloroplast; Lyase; Magnesium; Metal-binding; Plastid.
FT CHAIN 1..547
FT /note="Germacrene A synthase"
FT /id="PRO_0000454962"
FT MOTIF 300..304
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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"
SQ SEQUENCE 547 AA; 64111 MW; 16883AE37B323582 CRC64;
MAQQEAEIIR PLANFSPSLW GDQFIKNDSD AKVEDKISKT IEVLKEEVKS MLTATGTKMV
DTMNLIDTLE RLGVSYHFEH EIEEILQQFF NLNTDYNDEA YDLYTVATHF RLFRQHGHRI
TCADIFGRWR DENGKFHEGL KDDAKGLLSL YEASYLRTRG ETILDEALDF TTASLKSIAP
NLESPLRRQV EHALVQQLHW GNPRIEARNF ISLYEEYEDK DESLLRFAKL DYNLLQMMHK
EELHEVSRWW KELDLVAKLP YARDRVVECF FWAMGVYHEP QYSRARVMLT KTIAMTSIID
DTYDAYGTIE ELDIFTEAIE RWNVEEMKRL PEYIKPFYKA LLELYEQFEE ELAKEGRSYA
THYAIESLKE LVRSYHVEAK WFIQGYLPPF EEYLKNALIT CTYCYHTTTS LLGVESAVRE
DFEWLSKKPK MLVAGLLICR VIDDIATYEV EKDRGQIATG IESYMRDNGA TKEEAITKFF
EIANDAWKDI NEECMRPSPH SRDVLMRILN LERIIDVTYK GNEDGYTQPE KVLKPHIIAL
FVDPIQI
