TPS30_ARATH
ID TPS30_ARATH Reviewed; 604 AA.
AC Q9LH31;
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 30 {ECO:0000303|PubMed:12207221};
DE Short=AtTPS30 {ECO:0000303|PubMed:12207221};
DE EC=4.2.3.-;
GN Name=TPS30 {ECO:0000303|PubMed:12207221};
GN OrderedLocusNames=At3g32030 {ECO:0000312|Araport:AT3G32030};
GN ORFNames=T8O3.12 {ECO:0000312|EMBL:BAB01981.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Nakamura Y.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. III.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
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 and diterpene (C20) synthase
CC activity in vitro. {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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP002068; BAB01981.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77679.1; -; Genomic_DNA.
DR RefSeq; NP_189746.1; NM_114026.2.
DR AlphaFoldDB; Q9LH31; -.
DR SMR; Q9LH31; -.
DR STRING; 3702.AT3G32030.1; -.
DR PaxDb; Q9LH31; -.
DR PRIDE; Q9LH31; -.
DR ProteomicsDB; 232500; -.
DR EnsemblPlants; AT3G32030.1; AT3G32030.1; AT3G32030.
DR GeneID; 822955; -.
DR Gramene; AT3G32030.1; AT3G32030.1; AT3G32030.
DR KEGG; ath:AT3G32030; -.
DR Araport; AT3G32030; -.
DR TAIR; locus:2114414; AT3G32030.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q9LH31; -.
DR OMA; FDVICKE; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q9LH31; -.
DR BioCyc; ARA:AT3G32030-MON; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9LH31; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LH31; baseline and differential.
DR Genevisible; Q9LH31; 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:TAIR.
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..604
FT /note="Terpenoid synthase 30"
FT /id="PRO_0000403717"
FT MOTIF 356..360
FT /note="DDXXD motif; degenerate"
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"
SQ SEQUENCE 604 AA; 69812 MW; 1872DB8CBD44999F CRC64;
MAVARTVFGL GTLSYLHQAP LFLKTSQSLF PRPSLSLKPM KHDFVCVKAT TKSSTSDDLE
SGRPSILFSP SIWGDYFLSV SVDDSEFDDI AREIESVMKP YVRDRLISSH NSNKDKIRLI
HLLISLGISY YFESEIEMIL NKAFEELDMI IAEEDDLETI SIMFEVFRLY QHKMSCDSFV
RFKGEDGRLK ESLVGDVRGM LQLYQAAHLG TPSDQYIMEE AKSFTRNHLE SLVESTTIPP
HFSSHIRDAL YIDRYHNMEI LVARKYISFY EQEEGHDLTL LKFGKLSFNY CRLHYIQELK
TLTKWWKDQD IPSNLPCVRD RIVETYFPTL GLYFEPRFSL GRIIIAKMTI IVVALNDVCD
SYATYPEAKS LIDSLQRWDI EAIDELPNYS RIVLRLILET IGEIEREMKP RGRSASVQHT
IDETKSLGRA YLALSKWASE GYMPTFDEYM EVGEVTGGMD DFALYSFIAM EDCDEKPLYE
WFDSKPKILQ ALSVLYRINN DIVTYEREMS KGEVVNGVNS YMNQHGVTKE EAVEELRKMA
RDNYKIVMEE LLTITDVPRP VLVRCLNLAR LFDVFCKHGN DEFTYPHGNL KDLITSIFIH
PIPV
