TPS18_ARATH
ID TPS18_ARATH Reviewed; 605 AA.
AC Q9LUE2; Q84UU6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Terpenoid synthase 18;
DE Short=AtTPS18;
DE EC=4.2.3.-;
GN Name=TPS18; OrderedLocusNames=At3g14520; ORFNames=MIE1.2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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; AF497489; AAO85537.1; -; mRNA.
DR EMBL; AB023038; BAB02384.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75534.1; -; Genomic_DNA.
DR EMBL; BT053762; ACL13989.1; -; mRNA.
DR RefSeq; NP_188070.2; NM_112312.5.
DR PDB; 7BZB; X-ray; 2.15 A; A=1-605.
DR PDB; 7BZC; X-ray; 2.30 A; A=1-605.
DR PDBsum; 7BZB; -.
DR PDBsum; 7BZC; -.
DR AlphaFoldDB; Q9LUE2; -.
DR SMR; Q9LUE2; -.
DR STRING; 3702.AT3G14520.1; -.
DR PaxDb; Q9LUE2; -.
DR PRIDE; Q9LUE2; -.
DR ProteomicsDB; 228381; -.
DR EnsemblPlants; AT3G14520.1; AT3G14520.1; AT3G14520.
DR GeneID; 820677; -.
DR Gramene; AT3G14520.1; AT3G14520.1; AT3G14520.
DR KEGG; ath:AT3G14520; -.
DR Araport; AT3G14520; -.
DR TAIR; locus:2089536; AT3G14520.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q9LUE2; -.
DR OMA; IMGHEDE; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q9LUE2; -.
DR BioCyc; ARA:AT3G14520-MON; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9LUE2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUE2; baseline and differential.
DR Genevisible; Q9LUE2; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..605
FT /note="Terpenoid synthase 18"
FT /id="PRO_0000403709"
FT MOTIF 356..360
FT /note="DDXXD motif"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 42..44
FT /note="AKK -> VKR (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..232
FT /note="DSWIG -> ESWIA (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..278
FT /note="HNK -> YDE (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..294
FT /note="FCQFH -> LCQFR (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="T -> I (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="D -> H (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="V -> I (in Ref. 1; AAO85537)"
FT /evidence="ECO:0000305"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 84..106
FT /evidence="ECO:0007829|PDB:7BZB"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:7BZB"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:7BZB"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:7BZB"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7BZC"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 278..309
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 339..358
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 388..408
FT /evidence="ECO:0007829|PDB:7BZB"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 414..440
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 475..482
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 487..503
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 505..510
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 517..525
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 529..553
FT /evidence="ECO:0007829|PDB:7BZB"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 560..577
FT /evidence="ECO:0007829|PDB:7BZB"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:7BZB"
SQ SEQUENCE 605 AA; 69410 MW; D9421E680D144DE6 CRC64;
MDATRTFFGL PNVHNVPLCL TSNLSLFPQR LLQKHTLPLK PAKKHHLVCV RSTKSSDDLE
GSRPSTYFSP SLWGDHFLSV SLDRGEFDEL EREIETMKPL VKDMLMSSQS SDKEKIRLIH
LLVSLGSSYH FDKEIQDILK HSFTKLDDII VGEDDLETIS IMFEVFRLYG HKMSCDAFDR
FRGEDGRFKE SLAKDVRGML QLFEVAHLGT PSEDIMDEAS SFAQNHLDSW IGGNVSGATP
HLLKHIQNSL YIPRYCNIEV LVAREYISYY EQEEGHNKIL LKFAKLNFNF CQFHYIQELK
TLTKWWKDLD LASKLPYIRD RLVESHLGGL GPYFEPHYSL GRIIVAKIIM TMVVVDDTYD
AHATVPEVAV LTECLQRLNI GADDKLPDYL RTVLESVFEV MGEIEQEMRP KGRSYGVKQV
LERFKNVAKA DKQLTEWART GDVPSFDEYM KVGLVTAGMD GYAGYCFIGM EDVSEKEAFE
WLSSNPLIIQ ALNVMFRLAN DVGTYETEIN RGEVANGLNC YMKQYGVTKE EASQELRKIY
SNNKKVVMEE FMNSHDHVPR QVLLRCLNFA RLFDVMYTEG DGYSEPKGKI EHFMTSLYVH
PIPLS
