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TPS7_HEDCO
ID   TPS7_HEDCO              Reviewed;         593 AA.
AC   W6HUT3;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Monoterpene synthase 7, chloroplastic {ECO:0000303|PubMed:25056927};
DE            Short=HcTPS7 {ECO:0000303|PubMed:25056927};
DE   AltName: Full=Alpha-pinene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.- {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Alpha-terpinene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.115 {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Beta-phellandrene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.- {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Beta-pinene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.- {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Gamma-terpinene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.114 {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Myrcene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.15 {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Sabinene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.- {ECO:0000269|PubMed:25056927};
DE   AltName: Full=Terpinolene synthase {ECO:0000303|PubMed:25056927};
DE            EC=4.2.3.113 {ECO:0000269|PubMed:25056927};
DE   Flags: Precursor;
GN   Name=TPS7 {ECO:0000303|PubMed:25056927};
OS   Hedychium coronarium (White butterfly ginger-lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Hedychium.
OX   NCBI_TaxID=71610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX   PubMed=25056927; DOI=10.1007/s00425-014-2127-x;
RA   Yue Y., Yu R., Fan Y.;
RT   "Characterization of two monoterpene synthases involved in floral scent
RT   formation in Hedychium coronarium.";
RL   Planta 240:745-762(2014).
CC   -!- FUNCTION: Monoterpene synthase involved in the biosynthesis of volatile
CC       compounds present in floral scent (PubMed:25056927). Mediates the
CC       conversion of (2E)-geranyl diphosphate (GPP) into sabinene and sub-
CC       products such as alpha-thujene, alpha-pinene, beta-pinene, myrcene,
CC       alpha-phellandrene, alpha-terpinene, beta-phellandrene, gamma-terpinene
CC       and terpinolene (PubMed:25056927). Unable to use farnesyl diphosphate
CC       (FPP) as substrate (PubMed:25056927). {ECO:0000269|PubMed:25056927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene;
CC         Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027,
CC         ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC         Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.113;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate;
CC         Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC         ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = beta-pinene + diphosphate;
CC         Xref=Rhea:RHEA:25666, ChEBI:CHEBI:33019, ChEBI:CHEBI:50025,
CC         ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25667;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC         Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.15;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = alpha-terpinene + diphosphate;
CC         Xref=Rhea:RHEA:32563, ChEBI:CHEBI:10334, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.115;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32564;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = beta-phellandrene + diphosphate;
CC         Xref=Rhea:RHEA:25504, ChEBI:CHEBI:33019, ChEBI:CHEBI:48741,
CC         ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25505;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene;
CC         Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.114;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:25056927};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=26.49 uM for (2E)-geranyl diphosphate
CC         {ECO:0000269|PubMed:25056927};
CC         Vmax=928.92 pmol/sec/mg enzyme with (2E)-geranyl diphosphate as
CC         substrate {ECO:0000269|PubMed:25056927};
CC         Note=kcat is 0.057 sec(-1) with (2E)-geranyl diphosphate as
CC         substrate. {ECO:0000269|PubMed:25056927};
CC       pH dependence:
CC         Optimum pH is 7.5 (PubMed:25056927). Active at pH between 6.0 and 9.0
CC         (PubMed:25056927). {ECO:0000269|PubMed:25056927};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:25056927};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:25056927}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:25056927}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers, petals and sepals, but
CC       almost undetectable in vegetative organs.
CC       {ECO:0000269|PubMed:25056927}.
CC   -!- DEVELOPMENTAL STAGE: During flower development, first observed in
CC       petals after about 40 hours, with a sharp increase between 32 and 48
CC       hours, and a decrease during flower senescence.
CC       {ECO:0000269|PubMed:25056927}.
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|UniProtKB:Q40577}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; KF765488; AHJ57305.1; -; mRNA.
DR   SMR; W6HUT3; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0102903; F:gamma-terpinene synthase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050551; F:myrcene synthase activity; IDA:UniProtKB.
DR   GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR   GO; GO:0080015; F:sabinene synthase activity; IDA:UniProtKB.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
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; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..593
FT                   /note="Monoterpene synthase 7, chloroplastic"
FT                   /id="PRO_0000454954"
FT   MOTIF           348..352
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         352
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         352
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         499
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   593 AA;  68541 MW;  D4C65F6F448E4A7A CRC64;
     MSVSLSFAAS ATFGFRGGLG GFSRPAAAIK QWRCLPRIQC HSAEQSQSPL RRSGNYQPSI
     WTHDRIQSLT LSHTADEDDH GERIKLLKCQ TNKLMEEKKG EVGEQLQLID HLQQLGVAYH
     FKDEIKDTLR GFYASFEDIS LQFKDNLHAS ALLFRLLREN GFSVSEDIFK KFKDDQKGQF
     EDRLQSQAEG LLSLYEASYL EKDGEELLHE AREFTTKHLK NLLEEEGSLK PGLIREQVAY
     ALELPLNRRF QRLHTKWFIG AWQRDPTMDP ALLLLAKLDF NALQNMYKRE LNEVSRWWTD
     LGLPQKLPFF RDRLTENYLW AVVFAFEPDS WAFREMDTKT NCFITMIDDV YDVYGTLDEL
     ELFTDIMERW DVNAIDKLPE YMKICFLAVF NTVNDAGYEV MRDKGVNIIP YLKRAWAELC
     KMYMREARWY HTGYTPTLDE YLDGAWISIS GALILSTAYC MGKDLTKEDL DKFSTYPSIV
     QPSCMLLRLH DDFGTSTEEL ARGDVQKAVQ CCMHERKVPE AVAREHIKQV MEAKWRVLNG
     NRVAASSFEE YFQNVAINLP RAAQFFYGKG DGYANADGET QKQVMSLLIE PVQ
 
 
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