NES2_FRAAN
ID NES2_FRAAN Reviewed; 578 AA.
AC P0CV95;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=(3S,6E)-nerolidol synthase 2, chloroplastic/mitochondrial;
DE Short=FaNES2;
DE EC=4.2.3.48;
DE Flags: Precursor;
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).
CC -!- FUNCTION: Involved in monoterpene (C10) and sesquiterpene (C15)
CC biosynthesis. Converts geranyl diphosphate (GPP) into linalool and
CC farnesyl diphosphate (FPP) into nerolidol.
CC {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: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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15522848}.
CC Plastid, chloroplast {ECO:0000269|PubMed:15522848}.
CC -!- TISSUE SPECIFICITY: Not detected in leaves or green fruit.
CC {ECO:0000269|PubMed:15522848}.
CC -!- DEVELOPMENTAL STAGE: Barely expressed in ripe fruits.
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; AX529067; CAD57106.1; -; Unassigned_DNA.
DR AlphaFoldDB; P0CV95; -.
DR SMR; P0CV95; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; 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 Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Plastid; Transit peptide.
FT TRANSIT 1..29
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..578
FT /note="(3S,6E)-nerolidol synthase 2,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000407981"
FT MOTIF 332..336
FT /note="DDXXD motif"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 66203 MW; C84EC7685358E5BE CRC64;
MASSSRAFFK VFNPAPKSIP RIGQSNLMQL THKKQLPTFQ RRGIAEDSLL PSSTTPIKPM
NVETKHTRTM GDIFVQHCQK LELFRNVLRN VAELDALEGL NMIDAVQRLG IDFHFQREID
EILHKQMSNV SASDDLHEVA LRFRLLRQHG YFVPEDVFNN FKDSKGTFKQ VLGEDIKGLM
SLYEASQLGT EGEDTLVEAE KFSGHLLKTS LSHLDHHHAR IVGNTLRNPH HKSLASFMAR
NFFVTTQATN SWLNLLKDVA KTDFNMVRSL HQNEIVQISK WWKELGLAKE LKFARDQPQK
WYIWSMACLT DPKLSEERVE LTKPISFVYL IDDIFDVYGT LDDLILFTEA VNRWEITAID
HLPDYMKICF KALYDMTNEI SCKVYQKHGW NPLQSLKISW ASLCNAFLVE AKWFASGQLP
KSKEYLKNGI VSSGVNVVLV HMFFILGQNI TTKSVELLNE TPAMISSSAA ILRLWDDLGS
AKDENQDGND GSYVRCYLEE HEGCSIEEAR EKTINMISDE WKKLNRELLS PNPFPATITL
ASLNLARMIP LMYSYDGNQC LPSLKEYMKL MLYETVSM