TPS5_VITAC
ID TPS5_VITAC Reviewed; 800 AA.
AC A0A2K9RG07;
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=Kolavenyl diphosphate synthase TPS5, chloroplastic {ECO:0000303|PubMed:29315936};
DE EC=5.5.1.29 {ECO:0000269|PubMed:29315936};
DE AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:29315936};
DE Short=VacTPS5 {ECO:0000303|PubMed:29315936};
DE Flags: Precursor;
GN Name=TPS5 {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 kolavenyl 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=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-kolavenyl
CC diphosphate; Xref=Rhea:RHEA:54676, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:138311; EC=5.5.1.29;
CC Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54677;
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; MG696752; AUT77124.1; -; mRNA.
DR AlphaFoldDB; A0A2K9RG07; -.
DR SMR; A0A2K9RG07; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0106242; F:kolavenyl diphosphate 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: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; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..800
FT /note="Kolavenyl diphosphate synthase TPS5, chloroplastic"
FT /id="PRO_0000449311"
FT MOTIF 375..378
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
SQ SEQUENCE 800 AA; 91815 MW; 3B1CCA2C532376AA CRC64;
MSLAYSQATS LLLSSTTRGG VPSLMHIPAT NSPARINTGA TPFWKLPFPA RPLRQYKSIT
RARNQVILTA EKSVDVDTEK NTHHQKATAE TTRELVERIR WMLQNMDDGE LSVSPYDTAW
VALVEDIGGS GRPQFPTSLE WISNNQYPDG SWGDRKFLFY DRILNTLACV VALKTWNMHP
DKCEKGLKFI KENIHSLENE NEEYMPVGFE VAFPSLIETA KKLGIEIPDD SPGMKDIYAK
RHLKLKKIPM DLLHKMPTSL LFSLEGMKGL DWQKLLNLRF EGSFLSSPSS TAYALQHTKD
ELSLQYLLKA IKKFNGGVPN AYPVDMFEHL WSVDRLQRLG ISRYFEPEIE ECMKYAYRYW
TDKGICWARN TNVQDVDDSS MGFRLLRLHS FPVTIDAFKQ FEKGGEFCSI PGQSTHAITG
MYNIFRASQV LFPGDHILAD ARKYSAKFLH QKRVNEAIVD KWIITKDLPG EVGYALDVPF
YASLPRLEAR FFLEHYGGDD DVWIGKTLYR MLYVNCDTYL ELAKLDYNVC QAVHQHEWTN
IRRWYKDCSV GEFRLAERSL LRAYYIAAST VFEPERSGER LAWAKTAILL ETILSQKLHS
EEKHTVVDEF KHGSISISGN GRRHQTRISL AETLIYTVNQ LSSDIKQAHG RDIHQQLHHA
WQKWLTTWEG RGNLGEAEAE LLVRTLHLSS GLDESWFSHP KYQQLLEVTS KVCHQLRLFQ
NRKMHDPKGC TIDLVTGTTF QIEAGMQELV KLVFTKSSED LDAHTKQSFF AIARSFYYTA
YCDPEAIESH VDKVLFDKVV
