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TPS1_SORBI
ID   TPS1_SORBI              Reviewed;         541 AA.
AC   C5YHH7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Zingiberene synthase;
DE            Short=SbTPS1;
DE            EC=4.2.3.65;
GN   Name=TPS1; OrderedLocusNames=Sb07g004470;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF TYR-369; LEU-401 AND VAL-435,
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY HERBIVORY, AND 3D-STRUCTURE
RP   MODELING.
RX   PubMed=21880075; DOI=10.1111/j.1365-313x.2011.04771.x;
RA   Zhuang X., Koellner T.G., Zhao N., Li G., Jiang Y., Zhu L., Ma J.,
RA   Degenhardt J., Chen F.;
RT   "Dynamic evolution of herbivore-induced sesquiterpene biosynthesis in
RT   sorghum and related grass crops.";
RL   Plant J. 69:70-80(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623;
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA   Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
CC   -!- FUNCTION: Sesquiterpene synthase converting farnesyl diphosphate into
CC       two major products, zingiberene > beta-sesquiphellandrene, and five
CC       minor products, 7-epi-sesquithujene, sesquisabinene A, (E)-alpha-
CC       bergamotene, (E)-beta-farnesene and beta-bisabolene. Can also accept
CC       geranyl diphosphate as substrate, producing nine monoterpenes, with
CC       myrcene, limonene and alpha-terpinolene as the major products.
CC       {ECO:0000269|PubMed:21880075}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = alpha-zingiberene +
CC         diphosphate; Xref=Rhea:RHEA:28643, ChEBI:CHEBI:10115,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.65;
CC         Evidence={ECO:0000269|PubMed:21880075};
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: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated by herbivory. {ECO:0000269|PubMed:21880075}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EES13421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM000766; EES13421.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; C5YHH7; -.
DR   SMR; C5YHH7; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   InParanoid; C5YHH7; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000000768; Chromosome 7.
DR   ExpressionAtlas; C5YHH7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102884; F:alpha-zingiberene synthase activity; IEA:UniProtKB-EC.
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;
KW   Reference proteome.
FT   CHAIN           1..541
FT                   /note="Zingiberene synthase"
FT                   /id="PRO_0000418831"
FT   MOTIF           295..299
FT                   /note="DDXXD motif"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         439
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         369
FT                   /note="Y->S: No effect on zingiberene production, but
FT                   increased production of (E)-alpha-bergamotene and (E)-beta-
FT                   farnesene. Production of beta-sesquiphellandrene and
FT                   increased production of (E)-alpha-bergamotene and (E)-beta-
FT                   farnesene; when associated with V-401 or with V-401 and S-
FT                   435."
FT                   /evidence="ECO:0000269|PubMed:21880075"
FT   MUTAGEN         401
FT                   /note="L->V: Changed product specificity and production of
FT                   mainly beta-sesquiphellandrene. Production of beta-
FT                   sesquiphellandrene and increased production of (E)-alpha-
FT                   bergamotene and (E)-beta-farnesene; when associated with S-
FT                   369 or with S-369 and S-435."
FT                   /evidence="ECO:0000269|PubMed:21880075"
FT   MUTAGEN         435
FT                   /note="V->S: Production of mainly beta-sesquiphellandrene
FT                   and beta-bisabolene. Production of beta-sesquiphellandrene
FT                   and increased production of (E)-alpha-bergamotene and (E)-
FT                   beta-farnesene; when associated with S-369 and V-401."
FT                   /evidence="ECO:0000269|PubMed:21880075"
SQ   SEQUENCE   541 AA;  62891 MW;  D0F1194A7433940B CRC64;
     MAALQYNCDA GLAKAPTFHP SLWGDFFLTY QPPTAPQHVY MKERAELLKE EVREIVKGTN
     ELPKLLDLII TLQRLGLDNH YEIEIDEHLH FIYNSSCDVK DLNLVSLRFY LLRKNGYDVS
     SDVFLNFKDK DGNFASDDIR SLLSLYNAAY LRTHGEEVLD EAIIFTRRHL EAALTSLESK
     LADEVSLSLQ TPLFRRVRIL ETRNYIPIYE MEPSRNEAML EFAKLNFNLL QILYCEELKT
     VTAWWKQLNI ETDLSFIRDR IVEMHFWMAG ACSEPKYSLS RVILTKMTAF ITILDDIIDT
     HSTTEEGKLL AKAIDRCSQD ANEVLPDYMK HFYMFLLKTF DSCEDELGPN KRYRVFYLKE
     LLKILVRGYS QEIEWRDEHY VPETIDKHLE ISRVTVGAFQ LACSSFVGMG DIITKEVLDW
     LLTYPELLKC FTTFVRLSND ITSTKREQTG GHHASTVQCY MMEHSTTMHD ACEKIKGLIE
     DSWKDMMQLY LTPTEQSKVV AQTVVDFART GDYMYKKTDA FTFSHTIKDM IALLYVEPIL
     F
 
 
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