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TPSBE_ZINZE
ID   TPSBE_ZINZE             Reviewed;         554 AA.
AC   B1B1U4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Beta-eudesmol synthase;
DE            EC=4.2.3.68;
DE   AltName: Full=10-epi-gamma-eudesmol synthase;
DE            EC=4.2.3.84;
DE   AltName: Full=Alpha-eudesmol synthase;
DE            EC=4.2.3.85;
GN   Name=ZSS2;
OS   Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=311405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=18242187; DOI=10.1016/j.febslet.2008.01.020;
RA   Yu F., Harada H., Yamasaki K., Okamoto S., Hirase S., Tanaka Y., Misawa N.,
RA   Utsumi R.;
RT   "Isolation and functional characterization of a beta-eudesmol synthase, a
RT   new sesquiterpene synthase from Zingiber zerumbet Smith.";
RL   FEBS Lett. 582:565-572(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=15586673; DOI=10.1023/b:joec.0000042400.14451.08;
RA   Marsaro A.L., Souza R.C., Della Lucia T.M., Fernandes J.B., Silva M.F.,
RA   Vieira P.C.;
RT   "Behavioral changes in workers of the leaf-cutting ant Atta sexdens
RT   rubropilosa induced by chemical components of Eucalyptus maculata leaves.";
RL   J. Chem. Ecol. 30:1771-1780(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of beta-eudesmol, a
CC       sesquiterpene with antifungal activity and responsible for resistance
CC       of plants to ant attack. Produces mainly beta-eudesmol, but also
CC       smaller amounts of 10-epi-gamma-eudesmol, alpha-eudesmol and
CC       aristolene. {ECO:0000269|PubMed:15586673, ECO:0000269|PubMed:18242187}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = beta-eudesmol +
CC         diphosphate; Xref=Rhea:RHEA:29495, ChEBI:CHEBI:10417,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763;
CC         EC=4.2.3.68; Evidence={ECO:0000269|PubMed:18242187};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = 10-epi-gamma-eudesmol +
CC         diphosphate; Xref=Rhea:RHEA:30947, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:62514, ChEBI:CHEBI:175763;
CC         EC=4.2.3.84; Evidence={ECO:0000269|PubMed:18242187};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = alpha-eudesmol +
CC         diphosphate; Xref=Rhea:RHEA:30951, ChEBI:CHEBI:10278,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763;
CC         EC=4.2.3.85; Evidence={ECO:0000269|PubMed:18242187};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in rhizomes. Detected in stems, but not
CC       in leaves. {ECO:0000269|PubMed:18242187}.
CC   -!- INDUCTION: Peak of expression in summer. {ECO:0000269|PubMed:18242187}.
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}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AB247334; BAG12021.1; -; mRNA.
DR   EMBL; AB263738; BAG12022.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1B1U4; -.
DR   SMR; B1B1U4; -.
DR   KEGG; ag:BAG12021; -.
DR   BioCyc; MetaCyc:MON-14903; -.
DR   BRENDA; 4.2.3.68; 12510.
DR   BRENDA; 4.2.3.84; 12510.
DR   BRENDA; 4.2.3.85; 12510.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005737; C:cytoplasm; 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:0006952; P:defense response; IEA:UniProtKB-KW.
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; Plant defense.
FT   CHAIN           1..554
FT                   /note="Beta-eudesmol synthase"
FT                   /id="PRO_0000412250"
FT   MOTIF           305..309
FT                   /note="DDXXD motif"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  64382 MW;  3F8E932949B9EA22 CRC64;
     MEKQSLTFDG DEEAKIDRKS SKYHPSIWGD YFIQNSSLTH AKESTQRMIK RVEELKVQVK
     SMFKDTSDLL QLMNLINSIQ MLGLDYHFEN EIDEALRLIY EVDDKSYGLY ETSLRFQLLR
     QHGYHVSADI FNKFKDDNGS FISSLNGDAK GLLSLYNVSY LGTHGETILD EAKSFTKPQL
     VSLMSELEQS LAAQVSLFLE LPLCRRNKIL LARKYILIYQ EDAMRNNVIL ELAKLNFNLL
     QSLYQEELKK ISIWWNDLAF AKSLSFTRDR VVEGYYWVLT IYFEPQHSRA RVICSKVFAF
     LSIMDDIYDN YGILEECTLL TEAIKRWNPQ AIDGLPEYLK DYYLKLLKTF EEFEDELELN
     EKYRMLYLQD EVKALAISYL QEAKWGIERH VPSLDEHLHN SLISSGSSTV ICASFVGMGE
     VATKEVFDWL SSFPKVVEAC CVIGRLLNDI RSHELEQGRD HTASTVESYM KEHDTNVDVA
     CEKLREIVEK AWKDLNNESL NPTKVPRLMI ERIVNLSKSN EEIYKYNDTY TNSDTTMKDN
     ISLVLVESCD YFNK
 
 
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