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TPS17_ARATH
ID   TPS17_ARATH             Reviewed;         601 AA.
AC   Q9LRR2;
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 17;
DE            Short=AtTPS17;
DE            EC=4.2.3.-;
GN   Name=TPS17; OrderedLocusNames=At3g14490; ORFNames=MOA2.12;
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: Expressed exclusively in flowers.
CC       {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=BAB01341.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB028617; BAB01341.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75532.1; -; Genomic_DNA.
DR   RefSeq; NP_188067.1; NM_112309.2.
DR   AlphaFoldDB; Q9LRR2; -.
DR   SMR; Q9LRR2; -.
DR   STRING; 3702.AT3G14490.1; -.
DR   PaxDb; Q9LRR2; -.
DR   PRIDE; Q9LRR2; -.
DR   EnsemblPlants; AT3G14490.1; AT3G14490.1; AT3G14490.
DR   GeneID; 820672; -.
DR   Gramene; AT3G14490.1; AT3G14490.1; AT3G14490.
DR   KEGG; ath:AT3G14490; -.
DR   Araport; AT3G14490; -.
DR   TAIR; locus:2091687; AT3G14490.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   InParanoid; Q9LRR2; -.
DR   OMA; RLRGYYM; -.
DR   OrthoDB; 360509at2759; -.
DR   PhylomeDB; Q9LRR2; -.
DR   BioCyc; ARA:AT3G14490-MON; -.
DR   UniPathway; UPA00213; -.
DR   PRO; PR:Q9LRR2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LRR2; baseline and differential.
DR   Genevisible; Q9LRR2; 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 17"
FT                   /id="PRO_0000403708"
FT   MOTIF           354..358
FT                   /note="DDXXD motif; degenerate"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
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"
SQ   SEQUENCE   601 AA;  70179 MW;  F8382AFBB22CE84B CRC64;
     MEATRTSFGL HNAPLCPTTN PSLFPRRWLH KHTLSLKPAK QHHLVCVRAT ESNDNLESSR
     PLAHFSPTLW GDHFLSVPLH VAEFDDFSRE IEVTMKPKVR DMLKSSKNSD NERIRLIHLL
     MNLGIAYHFE IEIDEILGQA FGNLDDIIAK ENDLETISTM FEVFRLRGYY MPCYAFNRFK
     GEDGRFKESL AEDIRGMLQL YEAAHLGTPS EDIMDEALSF TRYRLESLTS NHTATASPHL
     SKHIQNALYR ARYHNLEILV AREYISFYEQ EEDHDETLLK FAKLNFNYCQ LHYIQELKDL
     TKWWKELDLA SKLPYIRDRI VEVYFGALAL YFEPRYSLGR IIVTKITMIV TVFNDTCDAY
     GTLPEVTSLV DSFQRWDLGD IEKLPSYVKI VFRGVFETLE EIEQEMRPQG RSRIVQVAVD
     EIKKLGKAYL AISKWARASH VPTFEEYMEF GMQTSMDHFA AYSFIAMEDC DENQTCEWYK
     SRPKMMEALN GVFRIKNDIN TFEQEMSRGE VAKGLNCYMK QHGVSKEEAI GEMNKIYSNY
     YKIIMEEYLT TTAVPRPILV RCLNVSRPIH HFYKERDEFT DPYFGMLKEV ITSLFIHPIP
     L
 
 
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