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TPSA_ARATH
ID   TPSA_ARATH              Reviewed;         591 AA.
AC   Q9ZUH4; B4F7R5; Q9FVI8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Tricyclene synthase, chloroplastic {ECO:0000305};
DE            EC=4.2.3.105 {ECO:0000269|PubMed:10700382};
DE   AltName: Full=(E)-beta-ocimene synthase 0e23 {ECO:0000303|PubMed:10700382};
DE            EC=4.2.3.106 {ECO:0000269|PubMed:10700382};
DE   AltName: Full=Myrcene synthase 1 {ECO:0000303|PubMed:10700382};
DE            EC=4.2.3.15 {ECO:0000269|PubMed:10700382};
DE   AltName: Full=Terpenoid synthase 10 {ECO:0000303|PubMed:10700382};
DE            Short=AtTPS10 {ECO:0000303|PubMed:10700382};
DE   Flags: Precursor;
GN   Name=TPS10 {ECO:0000303|PubMed:10700382};
GN   OrderedLocusNames=At2g24210 {ECO:0000312|Araport:AT2G24210};
GN   ORFNames=F27D4.12 {ECO:0000312|EMBL:AAD03382.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 37-591, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10700382; DOI=10.1006/abbi.1999.1669;
RA   Bohlmann J., Martin D., Oldham N.J., Gershenzon J.;
RT   "Terpenoid secondary metabolism in Arabidopsis thaliana: cDNA cloning,
RT   characterization, and functional expression of a myrcene/(E)-beta-ocimene
RT   synthase.";
RL   Arch. Biochem. Biophys. 375:261-269(2000).
RN   [5]
RP   INDUCTION BY HERBIVORY.
RX   PubMed=11710601; DOI=10.1023/a:1012213116515;
RA   Van Poecke R.M., Posthumus M.A., Dicke M.;
RT   "Herbivore-induced volatile production by Arabidopsis thaliana leads to
RT   attraction of the parasitoid Cotesia rubecula: chemical, behavioral, and
RT   gene-expression analysis.";
RL   J. Chem. Ecol. 27:1911-1928(2001).
RN   [6]
RP   IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA   Aubourg S., Lecharny A., Bohlmann J.;
RT   "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT   Arabidopsis thaliana.";
RL   Mol. Genet. Genomics 267:730-745(2002).
RN   [7]
RP   FUNCTION.
RX   PubMed=12624761; DOI=10.1007/s00425-002-0924-0;
RA   Faeldt J., Arimura G., Gershenzon J., Takabayashi J., Bohlmann J.;
RT   "Functional identification of AtTPS03 as (E)-beta-ocimene synthase: a
RT   monoterpene synthase catalyzing jasmonate- and wound-induced volatile
RT   formation in Arabidopsis thaliana.";
RL   Planta 216:745-751(2003).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=12566586; DOI=10.1105/tpc.007989;
RA   Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT   "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT   flowers.";
RL   Plant Cell 15:481-494(2003).
RN   [9]
RP   GENE FAMILY.
RX   PubMed=12777052; DOI=10.1023/a:1023005504702;
RA   Lange B.M., Ghassemian M.;
RT   "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT   in isoprenoid and chlorophyll metabolism.";
RL   Plant Mol. Biol. 51:925-948(2003).
RN   [10]
RP   INDUCTION BY METHYL JASMONATE.
RX   PubMed=16021335; DOI=10.1007/s11103-005-7306-5;
RA   Devoto A., Ellis C., Magusin A., Chang H.-S., Chilcott C., Zhu T.,
RA   Turner J.G.;
RT   "Expression profiling reveals COI1 to be a key regulator of genes involved
RT   in wound- and methyl jasmonate-induced secondary metabolism, defence, and
RT   hormone interactions.";
RL   Plant Mol. Biol. 58:497-513(2005).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=16297850; DOI=10.1016/j.abb.2005.09.019;
RA   Ro D.-K., Ehlting J., Keeling C.I., Lin R., Mattheus N., Bohlmann J.;
RT   "Microarray expression profiling and functional characterization of AtTPS
RT   genes: duplicated Arabidopsis thaliana sesquiterpene synthase genes
RT   At4g13280 and At4g13300 encode root-specific and wound-inducible (Z)-gamma-
RT   bisabolene synthases.";
RL   Arch. Biochem. Biophys. 448:104-116(2006).
RN   [12]
RP   INDUCTION BY HERBIVORY.
RX   PubMed=18400103; DOI=10.1186/1471-2164-9-154;
RA   Ehlting J., Chowrira S.G., Mattheus N., Aeschliman D.S., Arimura G.,
RA   Bohlmann J.;
RT   "Comparative transcriptome analysis of Arabidopsis thaliana infested by
RT   diamond back moth (Plutella xylostella) larvae reveals signatures of stress
RT   response, secondary metabolism, and signalling.";
RL   BMC Genomics 9:154-154(2008).
CC   -!- FUNCTION: Involved in monoterpene (C10) biosynthesis. The major product
CC       is beta-myrcene (56%) followed by (E)-beta-ocimene (20%) and minor
CC       amounts (less than 5%) of the cyclic monoterpene (-)-limonene, (+)-
CC       limonene, 2-carene and tricyclene. {ECO:0000269|PubMed:10700382,
CC       ECO:0000305|PubMed:12624761}.
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:10700382};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC         Evidence={ECO:0000269|PubMed:10700382};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = diphosphate + tricyclene;
CC         Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:64266; EC=4.2.3.105;
CC         Evidence={ECO:0000269|PubMed:10700382};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32688;
CC         Evidence={ECO:0000269|PubMed:10700382};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC         Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:64280; EC=4.2.3.106;
CC         Evidence={ECO:0000269|PubMed:10700382};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
CC         Evidence={ECO:0000269|PubMed:10700382};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O81192};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:O81192};
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 stroma {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in flowers but also in
CC       leaves, siliques and in stems. {ECO:0000269|PubMed:12566586,
CC       ECO:0000269|PubMed:16297850}.
CC   -!- INDUCTION: By methyl jasmonate. Also induced in response to the
CC       caterpillar P.xylostella or P.rapae feeding.
CC       {ECO:0000269|PubMed:11710601, ECO:0000269|PubMed:16021335,
CC       ECO:0000269|PubMed:18400103}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC005967; AAD03382.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07543.1; -; Genomic_DNA.
DR   EMBL; BT033153; ACF41947.1; -; mRNA.
DR   EMBL; AF178535; AAG09310.1; -; mRNA.
DR   PIR; H84633; H84633.
DR   RefSeq; NP_179998.1; NM_127982.4.
DR   AlphaFoldDB; Q9ZUH4; -.
DR   SMR; Q9ZUH4; -.
DR   STRING; 3702.AT2G24210.1; -.
DR   PaxDb; Q9ZUH4; -.
DR   PRIDE; Q9ZUH4; -.
DR   ProteomicsDB; 228334; -.
DR   EnsemblPlants; AT2G24210.1; AT2G24210.1; AT2G24210.
DR   GeneID; 816955; -.
DR   Gramene; AT2G24210.1; AT2G24210.1; AT2G24210.
DR   KEGG; ath:AT2G24210; -.
DR   Araport; AT2G24210; -.
DR   TAIR; locus:2047510; AT2G24210.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   HOGENOM; CLU_003125_7_1_1; -.
DR   OMA; KMINDMW; -.
DR   OrthoDB; 401091at2759; -.
DR   PhylomeDB; Q9ZUH4; -.
DR   BioCyc; MetaCyc:AT2G24210-MON; -.
DR   BRENDA; 4.2.3.106; 399.
DR   BRENDA; 4.2.3.15; 399.
DR   UniPathway; UPA00213; -.
DR   PRO; PR:Q9ZUH4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZUH4; baseline and differential.
DR   Genevisible; Q9ZUH4; AT.
DR   GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
DR   GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:TAIR.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050551; F:myrcene synthase activity; IDA:TAIR.
DR   GO; GO:0010333; F:terpene synthase activity; ISS:UniProtKB.
DR   GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:TAIR.
DR   GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
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   Reference proteome; Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..591
FT                   /note="Tricyclene synthase, chloroplastic"
FT                   /id="PRO_0000348417"
FT   MOTIF           339..343
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         343
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         484
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         488
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         492
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
SQ   SEQUENCE   591 AA;  69279 MW;  6637805072B2E9CD CRC64;
     MATLLQIGSG VIYSNALRKT LRRPQSSTCI IVTETTPCNK SPTVQRRSAN YQPSRWDHHH
     LLSVENKFAK DKRVRERDLL KEKVRKMLND EQKTYLDQLE FIDDLQKLGV SYHFEAEIDN
     ILTSSYKKDR TNIQESDLHA TALEFRLFRQ HGFNVSEDVF DVFMENCGKF DRDDIYGLIS
     LYEASYLSTK LDKNLQIFIR PFATQQLRDF VDTHSNEDFG SCDMVEIVVQ ALDMPYYWQM
     RRLSTRWYID VYGKRQNYKN LVVVEFAKID FNIVQAIHQE ELKNVSSWWM ETGLGKQLYF
     ARDRIVENYF WTIGQIQEPQ YGYVRQTMTK INALLTTIDD IYDIYGTLEE LQLFTVAFEN
     WDINRLDELP EYMRLCFLVI YNEVNSIACE ILRTKNINVI PFLKKSWTDV SKAYLVEAKW
     YKSGHKPNLE EYMQNARISI SSPTIFVHFY CVFSDQLSIQ VLETLSQHQQ NVVRCSSSVF
     RLANDLVTSP DELARGDVCK SIQCYMSETG ASEDKARSHV RQMINDLWDE MNYEKMAHSS
     SILHHDFMET VINLARMSQC MYQYGDGHGS PEKAKIVDRV MSLLFNPIPL D
 
 
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