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TPS15_ARATH
ID   TPS15_ARATH             Reviewed;         601 AA.
AC   Q9LS76;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Terpenoid synthase 15;
DE            Short=AtTPS15;
DE            EC=4.2.3.-;
GN   Name=TPS15; OrderedLocusNames=At3g29190; ORFNames=MXO21.3;
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=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   [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   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   [4]
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   [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 siliques but also in
CC       stems. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01815.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB026657; BAB01815.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE77550.1; -; Genomic_DNA.
DR   RefSeq; NP_189564.2; NM_113843.3.
DR   AlphaFoldDB; Q9LS76; -.
DR   SMR; Q9LS76; -.
DR   BioGRID; 7901; 1.
DR   PaxDb; Q9LS76; -.
DR   PRIDE; Q9LS76; -.
DR   ProteomicsDB; 228380; -.
DR   EnsemblPlants; AT3G29190.1; AT3G29190.1; AT3G29190.
DR   GeneID; 822572; -.
DR   Gramene; AT3G29190.1; AT3G29190.1; AT3G29190.
DR   KEGG; ath:AT3G29190; -.
DR   Araport; AT3G29190; -.
DR   TAIR; locus:2094827; AT3G29190.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   InParanoid; Q9LS76; -.
DR   OMA; HATIKEC; -.
DR   OrthoDB; 20156at2759; -.
DR   PhylomeDB; Q9LS76; -.
DR   BioCyc; ARA:AT3G29190-MON; -.
DR   UniPathway; UPA00213; -.
DR   PRO; PR:Q9LS76; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LS76; baseline and differential.
DR   Genevisible; Q9LS76; AT.
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..601
FT                   /note="Terpenoid synthase 15"
FT                   /id="PRO_0000403706"
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         498
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         506
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   601 AA;  69668 MW;  5A1C2A916AD51663 CRC64;
     MEVISIFGPK HGSLISLHSS YNLFKVSKVT RFRRTLFPSN HAKVFRFKAL TCDNQESNNM
     FKELPTSEWT HHFHSIQVDV SEMDAIRIEI DALKPKVKNI LMSFQGIDST KKRILMIYML
     ISLGLACQFE EEIYETLKEG FGKIEEMMAN EEDLYTVSII FWVFRRYGHY ISSDFFRRFK
     GNDGNFKKSL IGDAKGMLSF YEAANMATTK DYILDEALSF TSSHLESLAA NGACPPHMSR
     RIRNALNASQ HWNMEMLVAV EYISFYEKEK DHNEMLLKFS KLNFKFLQLQ YLQELKVLTK
     WYKEVDFVSK LPPYFRDRIV ENHFFIQTLF VESQHSRARI MMAKYFILLV IQDDTLDRYA
     SLPEAESLVN SLNRWAPDHA MDKQPDYLKF VFKFILDTFE EFEKELRPEG GSFGVCATIE
     EFKSLVKANL EAEKWALADN MPSFEEYIEV TGVGITAMTT LMGAMMCMGK IVPKEDYKWL
     KSRPKIIQAL AIKGRLMNDM KGYKEDMSRG YAANAVTCYM KQYRVTEQEA LKEFEKMVAV
     ANKTVNEEFL TTMGVSRLVL KLAMGVGLMI SITYSEDEGY THPEGKIKEK MTTLFVDQIP
     L
 
 
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