NES1_FRAAN
ID NES1_FRAAN Reviewed; 519 AA.
AC P0CV94;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=(3S,6E)-nerolidol synthase 1;
DE Short=FaNES1;
DE EC=4.2.3.48;
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Elsanta;
RA Aharoni A., Jongsma M.A., Verhoeven H.A., Bouwmeester H.J.;
RT "Isoprenoid synthases.";
RL Patent number WO02064764, 22-AUG-2002.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Elsanta;
RX PubMed=15522848; DOI=10.1105/tpc.104.023895;
RA Aharoni A., Giri A.P., Verstappen F.W., Bertea C.M., Sevenier R., Sun Z.,
RA Jongsma M.A., Schwab W., Bouwmeester H.J.;
RT "Gain and loss of fruit flavor compounds produced by wild and cultivated
RT strawberry species.";
RL Plant Cell 16:3110-3131(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14630967; DOI=10.1105/tpc.016253;
RA Aharoni A., Giri A.P., Deuerlein S., Griepink F., de Kogel W.J.,
RA Verstappen F.W., Verhoeven H.A., Jongsma M.A., Schwab W., Bouwmeester H.J.;
RT "Terpenoid metabolism in wild-type and transgenic Arabidopsis plants.";
RL Plant Cell 15:2866-2884(2003).
CC -!- FUNCTION: Involved in monoterpene (C10) and sesquiterpene (C15)
CC biosynthesis. Converts geranyl diphosphate (GPP) into S-linalool and
CC farnesyl diphosphate (FPP) into (3S)-E-nerolidol. Exclusively present
CC and highly expressed in the fruit of cultivated (octaploid) varieties.
CC {ECO:0000269|PubMed:14630967, ECO:0000269|PubMed:15522848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (3S,6E)-nerolidol +
CC diphosphate; Xref=Rhea:RHEA:27530, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59958, ChEBI:CHEBI:175763;
CC EC=4.2.3.48; Evidence={ECO:0000269|PubMed:14630967,
CC ECO:0000269|PubMed:15522848};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 uM for farnesyl diphosphate {ECO:0000269|PubMed:15522848};
CC KM=29.0 uM for geranyl diphosphate {ECO:0000269|PubMed:15522848};
CC Vmax=2.3 nmol/h/ug enzyme toward geranyl diphosphate
CC {ECO:0000269|PubMed:15522848};
CC Vmax=3.0 nmol/h/ug enzyme toward farnesyl diphosphate
CC {ECO:0000269|PubMed:15522848};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15522848}.
CC -!- TISSUE SPECIFICITY: Expressed in receptacle tissue. Not detected in
CC leaves or green fruit. {ECO:0000269|PubMed:15522848}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during fruit ripening.
CC {ECO:0000269|PubMed:15522848}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsg subfamily.
CC {ECO:0000305}.
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DR EMBL; AX528996; CAD57081.1; -; Unassigned_DNA.
DR EMBL; AX528998; CAD57082.1; -; Unassigned_DNA.
DR AlphaFoldDB; P0CV94; -.
DR SMR; P0CV94; -.
DR BRENDA; 4.2.3.48; 2320.
DR SABIO-RK; P0CV94; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..519
FT /note="(3S,6E)-nerolidol synthase 1"
FT /id="PRO_0000407980"
FT MOTIF 273..277
FT /note="DDXXD motif"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 519 AA; 59785 MW; 3B2F12324C1F4A5A CRC64;
MNVETKHTRT MGDIFVQHSQ KLELLKTVLR NVAELDALEG LNMIDAVQRL GIDYNFQREI
DEILHKQMSI VSARDDLHEV ALRFRLLRQH GYFVPEDVFN NFKDSKGTFK QVLGEDIKGL
MSLYEASQLG TEGEDILVEA EKFSGHLLKT SLSHLDHHRV RIVANTLRNP HHKSLAPFMA
RNFFVTSQAT NSWLNLLKEV AKTDFNMVRS LHQNEIVQMS KWWKELGLAK ELKFARDQPL
KWYIWSMACL TDPKLSEERV ELTKPISFVY LIDDIFDVYG TLDDLILFTE AVNRWEITAI
DHLPDYMKIC FKALYDMTNE FSSKVYLKHG WNPLQSLKIS WASLCNAFLV EAKWFASGKL
PKSEEYLKNG IVSSGVNVVL VHMFFLLGQN ITRKSVELLN ETPAIISSSA AILRLWDDLG
SAKDENQDGN DGSYVRCYLE EHEGCSIEEA REKTINMISD EWKKLNRELL SPNPFPASFT
LASLNLARMI PLMYSYDGNQ CLPSLKEYMK LMLYETVSM
