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NES1_FRAVE
ID   NES1_FRAVE              Reviewed;         580 AA.
AC   P0CV96;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=(3S,6E)-nerolidol synthase 1, chloroplastic;
DE            Short=FvNES1;
DE            EC=4.2.3.48;
DE   Flags: Precursor;
OS   Fragaria vesca (Woodland strawberry) (Potentilla vesca).
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=57918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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], MUTAGENESIS OF TRP-6 AND ILE-16,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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 S-linalool and
CC       farnesyl diphosphate (FPP) into (3S)-E-nerolidol (By similarity).
CC       Probably not expressed in wild strawberry species. {ECO:0000250}.
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;
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: Plastid, chloroplast
CC       {ECO:0000269|PubMed:15522848}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in red stage fruit tissue.
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; AX529002; CAD57084.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P0CV96; -.
DR   SMR; P0CV96; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; 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; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..580
FT                   /note="(3S,6E)-nerolidol synthase 1, chloroplastic"
FT                   /id="PRO_0000407982"
FT   MOTIF           334..338
FT                   /note="DDXXD motif"
FT   BINDING         334
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         482
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         486
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         6
FT                   /note="W->R: Dual targeting to mitochondrion and
FT                   chloroplast; when associated with I-16 deletion."
FT                   /evidence="ECO:0000269|PubMed:15522848"
FT   MUTAGEN         16
FT                   /note="Missing: Dual targeting to mitochondrion and
FT                   chloroplast; when associated with R-6."
FT                   /evidence="ECO:0000269|PubMed:15522848"
SQ   SEQUENCE   580 AA;  66532 MW;  557B6FFE25C61391 CRC64;
     MASSSWAFFK VFNPQIAPKS ISHIGQSDLM QLTHKKQLPT FQRRGIAEDS LLPSSTTPIK
     PMHVETKHTR TMGDIFVQHS QKLELFRNVL RNAAELDALE GLNMIDAVQR LGIDYHFQRE
     IDEILHKQMG IVSACDDLYE VALRFRLLRQ HGYFVPEDVF NNFKDSKGTF KQVLGEDIKG
     LMSLYEASQL GTEGEDTLVE AEKFSGHLLK TSLSHLDRHR ARIVGNTLRN PHRKSLASFM
     ARNFFVTSQA TNSWLNLLKE VAKTDFNMVR SVHQKEIVQI SKWWKELGLV KELKFARDQP
     LKWYTWSMAG LTDPKLSEER VELTKPISFV YLIDDIFDVY GTLDDLILFT EAVNRWEITA
     IDHLPDYMKI CFKALYDMTN EFSCKVYQKH GWNPLRSLKI SWASLCNAFL VEAKWFASGQ
     LPKSEEYLKN GIVSSGVNVG LVHMFFLLGQ NITRKSVELL NETPAMISSS AAILRLWDDL
     GSAKDENQDG NDGSYVRCYL EEHEGCSIEE AREKTINMIS DEWKKLNREL LSPNPFPATF
     TSASLNLARM IPLMYSYDGN QSLPSLKEYM KLMLYETVSM
 
 
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