TP20L_ARATH
ID TP20L_ARATH Reviewed; 592 AA.
AC A0A178U9Y5;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Bifunctional dolabella-3,7-dien-18-ol synthase/dolathalia-3,7,11-triene synthase TPS20, chloroplastic {ECO:0000305};
DE EC=4.2.3.167 {ECO:0000269|PubMed:27933080};
DE EC=4.2.3.168 {ECO:0000269|PubMed:27933080};
DE AltName: Full=Terpenoid synthase 20 {ECO:0000305};
DE Short=AtTPS20 {ECO:0000305};
DE Flags: Precursor;
GN Name=TPS20 {ECO:0000305};
GN OrderedLocusNames=AXX17_At5g46650 {ECO:0000312|EMBL:OAO90606.1};
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. Landsberg erecta;
RX PubMed=27354520; DOI=10.1073/pnas.1607532113;
RA Zapata L., Ding J., Willing E.M., Hartwig B., Bezdan D., Jiao W.B.,
RA Patel V., Velikkakam James G., Koornneef M., Ossowski S., Schneeberger K.;
RT "Chromosome-level assembly of Arabidopsis thaliana Ler reveals the extent
RT of translocation and inversion polymorphisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4052-E4060(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Cvi-0;
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 the biosynthesis of diterpenes in roots.
CC Possesses dolabella-3,7-dien-18-ol synthase activity and dolathalia-
CC 3,7,11-triene synthase activity in vitro. Catalyzes the formation of
CC dolabella-3,7-dien-18-ol and dolathalia-3,7,11-triene from
CC geranygeranyl diphosphate (GGPP). Does not seem to be involved in
CC sesquiterpene biosynthesis. {ECO:0000269|PubMed:27933080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = (3E,7E)-
CC dolabella-3,7-dien-18-ol + diphosphate; Xref=Rhea:RHEA:16345,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:137565; EC=4.2.3.167;
CC Evidence={ECO:0000269|PubMed:27933080};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (3E,7E)-dolathalia-
CC 3,7,11-triene + diphosphate; Xref=Rhea:RHEA:54040, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:138039; EC=4.2.3.168;
CC Evidence={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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.29 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:27933080};
CC Vmax=12.76 pmol/sec/mg enzyme toward geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:27933080};
CC Note=kcat is 0.00083 sec(-1) with geranylgeranyl diphosphate as
CC substrate. {ECO:0000269|PubMed:27933080};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:27933080}.
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 -!- CAUTION: TPS20 in Arabidopsis ecotype Columbia lacks dolabellane-type
CC diterpene synthase activity because of a 17 amino acid deletion and
CC several mutations in its sequence. TPS20 protein in ecotype Cvi is
CC functional and possesses dolabellane-type diterpene synthase activity.
CC {ECO:0000269|PubMed:27933080}.
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DR EMBL; LUHQ01000005; OAO90606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178U9Y5; -.
DR SMR; A0A178U9Y5; -.
DR BRENDA; 4.2.3.167; 399.
DR BRENDA; 4.2.3.168; 399.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000078284; Chromosome 5.
DR ExpressionAtlas; A0A178U9Y5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
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: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 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..592
FT /note="Bifunctional dolabella-3,7-dien-18-ol
FT synthase/dolathalia-3,7,11-triene synthase TPS20,
FT chloroplastic"
FT /id="PRO_0000442457"
FT MOTIF 349..353
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 592 AA; 69021 MW; E37EB9AC094C660F CRC64;
MEAITKNGSL SQTLVHCGPK SLSSFIPVRC LRFSKNPFPK KLVVTRARTS INSDHEAANR
PLFQFPPSLL DDRFLSISAN QSEIDSLGRD IEALKAKVSE KLVCMDVKER IHLIHLLVSL
GVAYHFEKQI EEFLKVDFEN VEDMNLGEED MYSISVIFRV FRLYRHKLSS DVFNRFKEEN
GDFKKCLLDD VRGMLSFYEA SYFGTNTEEI LDEAMGFTRK HLELFVGGSN EEHLSGHIKN
VLYLSQQENA EVVMSREYIQ FYEQETHHDE TLLKFAKINF KFMQLHYVQE LQTIVKWWKE
LDLESKIPNY YRVRAVECLY WAMAVYMEPQ YSVARIILSK SLVLWTIIDD LYDAYCTLPE
AIAFTENMER WETDAKDMPD HMKVLMRSFI DLHEDFKREV ILEGRLYSVE YGIDECKRLF
REDLKLSKWA RTGYIPNYDE YMEVGIVTAG IDMTVAFAFI GMGEAGKEAF DWIRSRPKFI
QTLDIKGRLR DDVATYKDEM ARGEIATGIN CYMKQYKVTE EEAFLEFHRR IKHTSKLVNE
EYFKTTVPLK LVRIAFNVGR AIDTNYKHGD GLTYGGIVEG QITSLFLDLI TI
