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TPS19_ARATH
ID   TPS19_ARATH             Reviewed;         602 AA.
AC   Q9LUE0; Q84UU5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Terpenoid synthase 19;
DE            Short=AtTPS19;
DE            EC=4.2.3.-;
GN   Name=TPS19; OrderedLocusNames=At3g14540; ORFNames=MIE1.4;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
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   [4]
RP   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   [5]
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).
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   -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and siliques but
CC       also in roots and leaves. {ECO:0000269|PubMed:12566586}.
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. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF497490; AAO85538.1; -; mRNA.
DR   EMBL; AB023038; BAB02386.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75536.1; -; Genomic_DNA.
DR   RefSeq; NP_188072.1; NM_112314.3.
DR   AlphaFoldDB; Q9LUE0; -.
DR   SMR; Q9LUE0; -.
DR   STRING; 3702.AT3G14540.1; -.
DR   PaxDb; Q9LUE0; -.
DR   PRIDE; Q9LUE0; -.
DR   ProteomicsDB; 245214; -.
DR   EnsemblPlants; AT3G14540.1; AT3G14540.1; AT3G14540.
DR   GeneID; 820680; -.
DR   Gramene; AT3G14540.1; AT3G14540.1; AT3G14540.
DR   KEGG; ath:AT3G14540; -.
DR   Araport; AT3G14540; -.
DR   TAIR; locus:2089631; AT3G14540.
DR   eggNOG; ENOG502SHPY; Eukaryota.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   InParanoid; Q9LUE0; -.
DR   OMA; YPISSDY; -.
DR   OrthoDB; 360509at2759; -.
DR   PhylomeDB; Q9LUE0; -.
DR   BioCyc; ARA:AT3G14540-MON; -.
DR   UniPathway; UPA00213; -.
DR   PRO; PR:Q9LUE0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LUE0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009975; F:cyclase activity; IBA:GO_Central.
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   GO; GO:0051762; P:sesquiterpene biosynthetic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..602
FT                   /note="Terpenoid synthase 19"
FT                   /id="PRO_0000403710"
FT   MOTIF           353..357
FT                   /note="DDXXD motif"
FT   BINDING         353
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         501
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         505
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        145
FT                   /note="G -> D (in Ref. 1; AAO85538)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396
FT                   /note="E -> K (in Ref. 1; AAO85538)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   602 AA;  69187 MW;  CC0E6384B26F480D CRC64;
     MEATRMGFGG LSVPLSLTPN LSLIPQRLLD KHNLSLKPVK IHHLVCVRST KSSDDLETSR
     PSTYFSPSLW GDHFLSVSLD HAEFVELERE IETMKPLVKD MLMSSQSSDK EKIRLIHLLV
     SLGSSYHFDK EIQDILKHSF TKLDGIIVEE DDLETISIMF EVFRLYGHKM SCDAFDRFRG
     GDGRFKESLA KDVRGMLQLF EVAHLGTLSE DIMDEALRFT RNHLESLTSG NVSSASPHIL
     KHIQNSLYIP RYCNIEVLVA REYISYYEQE EGYNEILLKF AKLNFNFCQC HYIQEIKTLT
     KWWKDLDLAS KLPYIRDRSV ESHLGGLGPY FEPQYSLGRI IVAKTIMIIV VADDTYDAHA
     TIPEATVLTE YFQRLNIGAD DKLSGYLRIV LESVFEVMGE IEQEMSPKGR SYSVKQVLER
     FKIIAKAYKQ LTEWARKGHV PTFDEYMKVG LVTAGMGDYA GYCFIGMEDI NEKEAFEWLN
     SNPLLIDALN VLFRIANDVG TYETEINRGE VANGLNCYMK QYGVTKEEAS RELRKMYIYN
     KKVVVEEFMN SHDRVPRQVL LRCLNFARLF DVIYTEGDGY SEPKGKIEHF MTSLYVHPIP
     LS
 
 
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