TPS2_VITAC
ID TPS2_VITAC Reviewed; 589 AA.
AC A0A2K9RFZ2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Class I diterpene synthase 2, chloroplastic {ECO:0000303|PubMed:29315936};
DE Short=VacTPS2 {ECO:0000303|PubMed:29315936};
DE AltName: Full=(13S)-vitexifolin A synthase {ECO:0000303|PubMed:29315936};
DE EC=4.2.3.- {ECO:0000269|PubMed:29315936};
DE AltName: Full=9,13-epoxylabda-14-ene synthase {ECO:0000303|PubMed:29315936};
DE EC=4.2.3.189 {ECO:0000269|PubMed:29315936};
DE AltName: Full=Viteagnusin D synthase {ECO:0000303|PubMed:29315936};
DE EC=4.2.3.- {ECO:0000269|PubMed:29315936};
DE Flags: Precursor;
GN Name=TPS2 {ECO:0000303|PubMed:29315936};
OS Vitex agnus-castus (Chaste tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Viticoideae; Vitex.
OX NCBI_TaxID=54477;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fruit, Leaf, and Trichome gland;
RX PubMed=29315936; DOI=10.1111/tpj.13822;
RA Heskes A.M., Sundram T.C.M., Boughton B.A., Jensen N.B., Hansen N.L.,
RA Crocoll C., Cozzi F., Rasmussen S., Hamberger B., Hamberger B., Staerk D.,
RA Moeller B.L., Pateraki I.;
RT "Biosynthesis of bioactive diterpenoids in the medicinal plant Vitex agnus-
RT castus.";
RL Plant J. 93:943-958(2018).
RN [2]
RP REVIEW ON MENSTRUAL CYCLE DISORDERS.
RX PubMed=12809367; DOI=10.1078/094471103322004866;
RA Wuttke W., Jarry H., Christoffel V., Spengler B., Seidlova-Wuttke D.;
RT "Chaste tree (Vitex agnus-castus)--pharmacology and clinical indications.";
RL Phytomedicine 10:348-357(2003).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid
CC including cleroda-dienols, and peregrinol lactones and furan
CC derivatives, dopaminergic diterpenoids that can bind to dopamine
CC receptors in the human pituitary gland, have probably ability to lower
CC prolactin levels, and are used to treat menstrual cycle disorders (e.g.
CC premenstrual syndrome and mastodynia) (Probable). Terpene synthase the
CC catalyzes the conversion of peregrinol diphosphate to viteagnusin D and
CC 9,13(R)-epoxy-labd-14-ene, and of syn-copalyl diphosophate to
CC vitexifolin A (PubMed:29315936). {ECO:0000269|PubMed:29315936,
CC ECO:0000305|PubMed:12809367, ECO:0000305|PubMed:29315936,
CC ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9alpha-copalyl diphosphate + H2O = (13S)-vitexifolin A +
CC diphosphate; Xref=Rhea:RHEA:40027, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58622, ChEBI:CHEBI:76954;
CC Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40028;
CC Evidence={ECO:0000269|PubMed:29315936};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene +
CC diphosphate; Xref=Rhea:RHEA:54512, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138232, ChEBI:CHEBI:138233; EC=4.2.3.189;
CC Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54513;
CC Evidence={ECO:0000269|PubMed:29315936};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + peregrinol diphosphate = diphosphate + viteagnusin D;
CC Xref=Rhea:RHEA:62180, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138232, ChEBI:CHEBI:145543;
CC Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62181;
CC Evidence={ECO:0000269|PubMed:29315936};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in trichomes of leaves and fruits.
CC {ECO:0000269|PubMed:29315936}.
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:0000250|UniProtKB:G8GJ94}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; MG696749; AUT77121.1; -; mRNA.
DR AlphaFoldDB; A0A2K9RFZ2; -.
DR SMR; A0A2K9RFZ2; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0062204; F:(13S)-vitexifolin A synthase activity; IDA:UniProtKB.
DR GO; GO:0106239; F:9,13-epoxylabda-14-ene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0062203; F:Viteagnusin D synthase activity; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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 SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..589
FT /note="Class I diterpene synthase 2, chloroplastic"
FT /id="PRO_0000449308"
FT MOTIF 328..332
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:G8GJ94"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 589 AA; 68332 MW; 994423B2B9DA3FA2 CRC64;
MSLRFNLIVT PFSNHRIRNR RETFPAQEFP VATSKSAVKV KCNLITSTDL VGKVREKING
KVDNSLEVPA IHPVDIPSNL CMIDTLERLG VDRYFQSEID GVLEETYRLW QQKEKDIFAD
VTCRAMAFRL LRVKGYEVSS DELAPYADQA HVNLQISDVT AVIELYRASQ ERIYEEESTL
EKLHAWTSTY LKQQLVSGTI SDKKLHKQVE YYLKNYHGIL DLVGIRRSLD LYDIDHYQIL
KAADRFRTIC KDLLAFSRQD FNNCQAQYQR ELQLLQRWYE DCRLDKLNYG RDVLRISYFV
SSAIIGDPEL SDARLAFAKY CVLTTCIDDF FDHAGSREES YRILELVKEW KEKPAEDYGS
KEVEFLFTAV YNTVNELAEM AYVEQGRCVK SLLIKLWVEL LTSFKKELDS WTDDTALSLD
EYLSSSWVSI TSRINILTSI QFLGLKLSEE MLSSQECTDL CRHGSLVVRL LNDMQTFEKE
RRENTKNSVS ILLEAPKHEG AITEEEVISK IKEIVEQNRR KLMQMVYQRG TIFPRKCKDV
FLKSCRGGYY LYSNGDEFTS PVQIMEDMKL CYEPLTFHPL EANNGGNKN
