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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
 
 
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