GEAS_LAVST
ID GEAS_LAVST Reviewed; 542 AA.
AC T1RRS0;
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=LsGEAS {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 stoechas (Butterfly 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=39333;
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 at low levels in leaves.
CC {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; JX501516; AGN72803.1; -; mRNA.
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..542
FT /note="Germacrene A synthase"
FT /id="PRO_0000454964"
FT MOTIF 295..299
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 542 AA; 63755 MW; 02B5AAD53D598CD7 CRC64;
MAQQEAEILR PLANFSPSLW GDQFIKNDSD AKVRYIFHYV DYTNLSMLTA TGTKMVDTMN
LIDTLERLGV SYHFEHEIEE ILQQFFNLNT DYNDEAYDLY TVATHFRLFR QHGHRITCDI
FGRWRDENGK FHEGLKDDAK GLLSLYEASY LRTRGETILD EALDFTTASL KSIAPNLESP
LRRQVEHALV QQLHWGNPRI EARNFISLYE EYEDKDESLL RFAKLDYNLL QMMHKEELHE
VSRWWKELDL VAKLPYARDR VVECFFWAMG VYHEPQYSRA RVMLTKTIAM TSIIDDTYDA
YGTIEELDIF TEAIERWNVE EMKRLPEYIK PFYKALLELY EQFEEELAKE GRSYATHYAI
ESLKELVRSY HVEAKWFIQG YLPPFEEYLK NALITCTYCY HTTTSLLGVE SAVREDFEWL
SKKPKMLVAG LLICRVIDDI ATYEVEKDRG QIATGIESYM RDNGATKEEA ITKFFEIAND
AWKDINEECM RPSPHSRDVL MRILNLERII DVTYKGNEDG YTQPEKVLKP HIIALFVDPI
QI
