TPS6_VITAC
ID TPS6_VITAC Reviewed; 594 AA.
AC A0A2K9RFZ9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Class I diterpene synthase TPS6, chloroplastic {ECO:0000303|PubMed:29315936};
DE AltName: Full=Labd-13(16),14-diene-9-ol synthase {ECO:0000303|PubMed:29315936};
DE EC=4.2.3.- {ECO:0000269|PubMed:29315936};
DE AltName: Full=Syn-isopimara-7,15-diene synthase {ECO:0000303|PubMed:29315936};
DE EC=4.2.3.- {ECO:0000269|PubMed:29315936};
DE AltName: Full=Terpene synthase 6 {ECO:0000303|PubMed:29315936};
DE Short=VacTPS6 {ECO:0000303|PubMed:29315936};
GN Name=TPS6 {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 labda-13(16),14-
CC dien-9-ol, and of syn-copalyl diphosophate to dehydroabietadiene and
CC syn-isopimara-7,15-diene (PubMed:29315936).
CC {ECO:0000269|PubMed:29315936, ECO:0000305|PubMed:12809367,
CC ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peregrinol diphosphate = diphosphate + labd-13(16),14-diene-9-
CC ol; Xref=Rhea:RHEA:62184, ChEBI:CHEBI:33019, ChEBI:CHEBI:138232,
CC ChEBI:CHEBI:145549; Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62185;
CC Evidence={ECO:0000269|PubMed:29315936};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9alpha-copalyl diphosphate = diphosphate + syn-isopimara-7,15-
CC diene; Xref=Rhea:RHEA:62188, ChEBI:CHEBI:33019, ChEBI:CHEBI:58622,
CC ChEBI:CHEBI:145566; Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62189;
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
CC {ECO:0000305|PubMed:29315936}.
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; MG696753; AUT77125.1; -; mRNA.
DR AlphaFoldDB; A0A2K9RFZ9; -.
DR SMR; A0A2K9RFZ9; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0062202; F:Labd-13(16),14-diene-9-ol synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0106243; F:syn-isopimara-7,15-diene 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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid.
FT CHAIN 1..594
FT /note="Class I diterpene synthase TPS6, chloroplastic"
FT /id="PRO_0000449312"
FT MOTIF 330..334
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:G8GJ94"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 594 AA; 69281 MW; 24C183A37ED574D9 CRC64;
MSLRFNLIVT PFSNYEIRNR RETFPVQKFL MTTSKSAIKV KCSLKTSIDL VGKIREKING
KVDNSLEVPT INYLVDIPSN LCMIDSLERL GVARYFQSEI DGVLEKTYRL WQQREKDIFA
DVTCRAMAFR FLRVKGYEVS SDELAPYADQ VHVNPQISDV TTVVELYRAS QVRIYEEDSI
LEKLHAWTST FLKQQLQSKT ISDKKLHEQV EYYLKNYHGI QNQVAVRRSL DLYDIDHYPI
LKVADRFRII YNEDFFVFLR QDFNLCQAQH QKELQQLQRW YEDCRLDTLN YGRNVVHVSC
FLAAANFGDP ELSNARLAFA KTIVLVTRID DFFDLAGSRE ESYKILELVK EWKEKPTEDY
GSKEVEILFT ALYDTVNEFA EIAYIEQGRC VKPLLIKLWV ELLTSFKKEL DSWTDDTALT
LDEYLSSAWM SIACRVCTLT ALQFLGVKLS EEMLSSQECT DLCRHLSFVN RLLNDVQTFE
RERKENTINA VSVLLAAHRH ERAITEEEAI SKIQEIVEQN RRKLMRMVYQ RESVFPRKCR
NVFLEVSKMG HYLYASGDEL TTPQQLMEDM KSLVFEPLAL HPLETNNVIA SGKN
