GEAS_LAVVI
ID GEAS_LAVVI Reviewed; 543 AA.
AC T1RRJ6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Germacrene A synthase {ECO:0000303|PubMed:24943828};
DE Short=LvGEAS {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 viridis (Green 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=1343918;
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: Barely detectable 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; JX501519; AGN72806.1; -; mRNA.
DR SMR; T1RRJ6; -.
DR BRENDA; 4.2.3.23; 13953.
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..543
FT /note="Germacrene A synthase"
FT /id="PRO_0000454963"
FT MOTIF 296..300
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
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 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 543 AA; 63826 MW; BFA4D533D0598F65 CRC64;
MAQQEAEILR PLANFSPSLW GDQFIKNDSD AKVRYIFHYV DYTNLSMLTA TGTKMVDTMN
LIDTLERLGV SYHFEHEIEE ILQQFFNLNT DYNDEAYDLY TVATHFRLFR QHGHRITCAD
IFGRWRDENG KFHEGLKDDA KGLLSLYEAS YLRTRGETIL DEALDFTTAS LKSIAPNLES
PLRRQVEHAL VQQLHWGNPR IEARNFISLY EEYEDKDESL LRFAKLDYNL LQMMHKEELH
EVSRWWKELD LVAKLPYARD RVVECFFWAM GVYHEPQYSR ARVMLTKTIA MTSIIDDTYD
AYGTIEELDI FTEAIERWNV EEMKRLPEYI KPFYKALLEL YEQFEEELAK EGRSYATHYA
IESLKELVRS YHVEAKWFIQ GYLPPFEEYL KNALITCTYC YHTTTSLLGV ESAVREDFEW
LSKKPKMLVA GLLICRVIDD IATYEVEKDR GQIATGIESY MRDNGATKEE AITKFFEIAN
DAWKDINEEC MRPSPHSRDV LMRILNLERI IDVTYKGNED GYTQPEKVLK PHIIALFVDP
IQI
