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TPS1_VITAC
ID   TPS1_VITAC              Reviewed;         798 AA.
AC   A0A2K9RFZ7;
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=Peregrinol diphosphate synthase TPS1, chloroplastic {ECO:0000303|PubMed:29315936};
DE            EC=4.2.1.174 {ECO:0000269|PubMed:29315936};
DE   AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:29315936};
DE            Short=VacTPS1 {ECO:0000303|PubMed:29315936};
DE   Flags: Precursor;
GN   Name=TPS1 {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 that
CC       produces peregrinol diphosphate from geranylgeranyl diphosphate (GGPP)
CC       (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=peregrinol diphosphate = (2E,6E,10E)-geranylgeranyl
CC         diphosphate + H2O; Xref=Rhea:RHEA:54652, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58756, ChEBI:CHEBI:138232; EC=4.2.1.174;
CC         Evidence={ECO:0000269|PubMed:29315936};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54654;
CC         Evidence={ECO:0000269|PubMed:29315936};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q38802};
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-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity, presumably through binding to Mg(2+). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; MG696748; AUT77120.1; -; mRNA.
DR   AlphaFoldDB; A0A2K9RFZ7; -.
DR   SMR; A0A2K9RFZ7; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0106238; F:peregrinol diphosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Isomerase; Lyase; Magnesium; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..798
FT                   /note="Peregrinol diphosphate synthase TPS1, chloroplastic"
FT                   /id="PRO_0000449307"
FT   MOTIF           377..380
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         379
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         463
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   798 AA;  92226 MW;  20083B50500EB797 CRC64;
     MASLSTPNIN NTTFVNSKTQ LPAVKVHLQK CYVGPWLNRG SKHMFTNYQF GHRQISKVAK
     YQASPDVVQV CDKVEHSTAQ SFELVDKKIE DNIRYVKELL NSIDDGHISV SAYDTAWFAL
     IRDLDGRDCP QFPSTIEWIA DNQLADGSWG DEDFYSAYDR LINTLACVLA LRTWNVHPEK
     SEKGISYIKE NLHELEDAEA ENMTCAFELL FPVLLKRAEN LGINEIPYDA PIIKEIYNIR
     DTKLTRIPLE VLHERSTSIL YGMEGLENLD LDWQKLMKLQ TPEGSFLTSP AATAFAFMYT
     KDENCLKYIK YILDKFNGAA VDVYPVDLFA RLWAVDRLQR LGISRFFESE IKDCLSYVHR
     FWTEKGIFSG RHALFHDLDD TSMGFRLLRQ HGYDMDPNVF KHFQKDGRFH CLGGDMSDSL
     TVTYNLYRAS QTQFPGEEIL EEARNFCYNF LQDRAARNQL VDKWVISKHL ADEMRTGLQL
     PWYASLPRVE ARYYLQHYAG SGDVWLGKNF FRMEDISNDK YKEIAKLDFS RCQAQHQFEW
     TYMQGWYESS NVQEFGISRK DLLVAYFLAA ATIFERERTK ERIVWAKSHI VSRMIKSFFT
     NETTSLEEKV ALLTGFEDNI NGLHKITSAK REHEHVDILL ATLHQLLGEF DEYASHQLKN
     AWRVWLTKLE QGEAGAEAEL LVTTLNICAG HDIAFKEDIL SQNEYKTLSN LTNKICQQLT
     QIQNKKVMET NDSNSIQDKE IEHDMQALVK SVLEEAVGID RNIKQTFLSV AKTYYYGAYI
     AAETIDVHIF KVLFEPVI
 
 
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