TPS25_ARATH
ID TPS25_ARATH Reviewed; 603 AA.
AC Q9LIA1; Q84UU7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Terpenoid synthase 25 {ECO:0000303|PubMed:12207221};
DE Short=AtTPS25 {ECO:0000303|PubMed:12207221};
DE EC=4.2.3.-;
GN Name=TPS25 {ECO:0000303|PubMed:12207221};
GN OrderedLocusNames=At3g29410 {ECO:0000312|Araport:AT3G29410};
GN ORFNames=MUO10.2 {ECO:0000312|EMBL:BAB02588.1};
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 [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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=27933080; DOI=10.3389/fpls.2016.01761;
RA Wang Q., Jia M., Huh J.H., Muchlinski A., Peters R.J., Tholl D.;
RT "Identification of a dolabellane type diterpene synthase and other root-
RT expressed diterpene synthases in Arabidopsis.";
RL Front. Plant Sci. 7:1761-1761(2016).
CC -!- FUNCTION: Involved in terpene biosynthesis in roots. Possesses
CC sesquiterpene (C15) synthase activity in vitro. Does not seem to be
CC involved in diterpene (C20) biosynthesis.
CC {ECO:0000269|PubMed:27933080}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots but also in
CC flowers. {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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02588.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX822709; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF497488; AAO85536.1; -; mRNA.
DR EMBL; AP001309; BAB02588.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77582.1; -; Genomic_DNA.
DR EMBL; BX822709; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_189587.1; NM_113867.5.
DR AlphaFoldDB; Q9LIA1; -.
DR SMR; Q9LIA1; -.
DR STRING; 3702.AT3G29410.1; -.
DR PaxDb; Q9LIA1; -.
DR PRIDE; Q9LIA1; -.
DR ProteomicsDB; 232497; -.
DR EnsemblPlants; AT3G29410.1; AT3G29410.1; AT3G29410.
DR GeneID; 822602; -.
DR Gramene; AT3G29410.1; AT3G29410.1; AT3G29410.
DR KEGG; ath:AT3G29410; -.
DR Araport; AT3G29410; -.
DR TAIR; locus:2093812; AT3G29410.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q9LIA1; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q9LIA1; -.
DR BioCyc; ARA:AT3G29410-MON; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9LIA1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIA1; baseline and differential.
DR Genevisible; Q9LIA1; 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; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IBA:GO_Central.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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..603
FT /note="Terpenoid synthase 25"
FT /id="PRO_0000403713"
FT MOTIF 356..360
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 31..32
FT /note="CR -> RC (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="Y -> D (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> N (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..73
FT /note="FSPSY -> YSPSL (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..87
FT /note="SIDDSE -> PIDESK (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="T -> S (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> M (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..235
FT /note="PLAGT -> SLVSH (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..248
FT /note="KHVENV -> NHVQNE (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> E (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="Q -> H (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="E -> D (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 325..333
FT /note="TYLGGLGVL -> VYLGSLGMF (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="L -> S (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..352
FT /note="LIM -> MIL (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="A -> S (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="Q -> K (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="F -> L (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="Q -> K (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="S -> N (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="F -> Y (in Ref. 1; AAO85536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 70225 MW; 95E1392AC42505E8 CRC64;
MEASKCFGPR TLPIIHNVPL CLKTNFSLFP CRLLQSQSLS SKKSTKHYLF RVKAETSGDL
ESTRPLTYFS PSYWGDHFLS VSIDDSEFEA LEKEIETVFK PKVRDMLMSP HSSDKERIRL
IHLLISLGIA YYYENEIEEI LHKAYGKLAC LISDEDDLET IAIMFEVFRL YGHKMPCDVF
ERFKSEDGKF KESLVGDVRG LLQLYEAAHL GAPSEDIMDE ALSFARYHLE PLAGTETSSN
LFKHVENVLY RARYHSIEIL VARQYISFYD QEEDQDETLL RFSKLNFNFC QMHYVKELKI
VTRWWKELGI ASKLPYSIRE RNVETYLGGL GVLFEPRYSL ARIFLAKLTL IMTVVDDTCD
AYATLPEVQS LHDAFHRWDL RAMEELPRYM RIIYQSVFET VEDIDREMIA RGKHGRLQLT
IDEIKSLMIW YLGIAKWARS DQVPSFEDYM EIGTPSSALD DFASYGFIAM DDCDQKQLKE
WFYSKPKIFH ALNALFRIRN DIVTFEQEMS RGEVANGVNC YMKQHGVTKE AAVEELRKME
RESYKIMIEE FMTSKAMPRQ ILVRPVNIAR VMDLFYKEAD GFGHPDQKLL QLIASLFLHP
IPL
