FENS_LAVVI
ID FENS_LAVVI Reviewed; 594 AA.
AC T1RR72;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=(-)-endo-fenchol synthase, chloroplastic {ECO:0000303|PubMed:24943828};
DE Short=Alpha fenchol synthase {ECO:0000303|PubMed:24943828};
DE Short=LvFENS {ECO:0000303|PubMed:24943828};
DE EC=4.2.3.10 {ECO:0000269|PubMed:24943828};
DE AltName: Full=Alpha pinene synthase {ECO:0000303|PubMed:24943828};
DE EC=4.2.3.- {ECO:0000269|PubMed:24943828};
DE AltName: Full=Limonene synthase {ECO:0000303|PubMed:24943828};
DE EC=4.2.3.- {ECO:0000269|PubMed:24943828};
DE Flags: Precursor;
GN Name=FENS {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: Monoterpene synthase involved in the biosynthesis of volatile
CC compounds widely used in aromatherapy and folk medicine, and present in
CC culinary herbs (PubMed:24943828). Mediates the conversion of (2E)-
CC geranyl diphosphate (GPP) into alpha fenchol, limonene and alpha-pinene
CC and, as minor compounds, into beta-myrcene, alpha-terpinolene and
CC alpha-phellandrene (PubMed:24943828). {ECO:0000269|PubMed:24943828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:24943828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC Evidence={ECO:0000269|PubMed:24943828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (1S,2S,4R)-endo-fenchol +
CC diphosphate; Xref=Rhea:RHEA:20565, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15405, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.10;
CC Evidence={ECO:0000269|PubMed:24943828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20566;
CC Evidence={ECO:0000269|PubMed:24943828};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + limonene;
CC Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:24943828};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX501517; AGN72804.1; -; mRNA.
DR SMR; T1RR72; -.
DR BRENDA; 4.2.3.10; 13953.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050437; F:(-)-endo-fenchol 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:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0046248; P:alpha-pinene biosynthetic process; 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:0046250; P:limonene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid 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; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..594
FT /note="(-)-endo-fenchol synthase, chloroplastic"
FT /id="PRO_0000454957"
FT MOTIF 348..352
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 594 AA; 69402 MW; 65C7B88373824AE6 CRC64;
MSSLVMHVGI VNKPAITYLP TLSRSASNLH NVSSTRLQTS CSLQLDYKPV DETRRSGNYQ
PSAWDFEYIQ SLKNKYKEEK YLTRHTKLTV QVKMLLDEDM EAVQQLDFIE DLNNLGISYL
FKDKITQILN HIYNEHRCFH NNEAEESDLY FTALGFRLLR QHGFKVSQEV FDCFKNEKYT
NFKASLAGDT KGLLQLYEAS FLLREGEDTL ELARKFSTKL LQQKIDEGEP DNNLLSCIRH
SLELPLHWRL QRLEARWFLD AYATRHDMNP IIFELAKLEF NITQATQQEE LKDLSRWWNS
TGLAEKLPFA RDRIVESYFW AMGTFEPHQY GYQRELVSKI IALTTVVDDI YDVYGTLEEL
ELFTDVIRRW ETESIDELPY YIQLCYLAVN KFVFDLAHDV LKDKGFNSLP YLKRSWKDLI
ERYLIEAKWY HNRYTPSLEE YLNNARVTIT CPTILSQIYF ALASPIEKPV IEVMYKYHDI
LYLSGMLLRL PDDLGTAPFE LKRGDVPKAV QCYMKERNVP EKEAREHVRF LIREASKQMN
TAMAIDCPFT EDFAVAAANL GRVANLAYVE GDGFGIQHSN IYEHIGSLMF KPYA
