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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}.
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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
 
 
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