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KS2_STERE
ID   KS2_STERE               Reviewed;         784 AA.
AC   Q9XEI0;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ent-kaurene synthase 2, chloroplastic {ECO:0000303|PubMed:10504563};
DE            Short=SrKS2 {ECO:0000303|PubMed:10504563};
DE            EC=4.2.3.19 {ECO:0000269|PubMed:10504563};
DE   Flags: Precursor;
GN   Name=KS22-1 {ECO:0000303|PubMed:10504563};
OS   Stevia rebaudiana (Stevia) (Eupatorium rebaudianum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Eupatorieae; Stevia.
OX   NCBI_TaxID=55670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Leaf;
RX   PubMed=10504563; DOI=10.1046/j.1365-313x.1999.00531.x;
RA   Richman A.S., Gijzen M., Starratt A.N., Yang Z., Brandle J.E.;
RT   "Diterpene synthesis in Stevia rebaudiana: recruitment and up-regulation of
RT   key enzymes from the gibberellin biosynthetic pathway.";
RL   Plant J. 19:411-421(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids
CC       natural products such as oridonin, miltiradiene, eriocalyxin B and
CC       nezukol, known to exhibit antitumor, anti-inflammatory and
CC       antibacterial activities, and in the production of gibberellins
CC       phytohormones (PubMed:10504563). Catalyzes the conversion of ent-
CC       copalyl diphosphate (ent-CPP) to ent-kaurene (PubMed:10504563).
CC       {ECO:0000269|PubMed:10504563}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC         Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58553; EC=4.2.3.19;
CC         Evidence={ECO:0000269|PubMed:10504563};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
CC         Evidence={ECO:0000269|PubMed:10504563};
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: Plant hormone biosynthesis; gibberellin biosynthesis.
CC       {ECO:0000305}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:10504563}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Accumulates in leaves.
CC       {ECO:0000269|PubMed:10504563}.
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. {ECO:0000305}.
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DR   EMBL; AF097311; AAD34295.1; -; mRNA.
DR   AlphaFoldDB; Q9XEI0; -.
DR   SMR; Q9XEI0; -.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009899; F:ent-kaurene synthase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0033332; P:ent-kaurene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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   SUPFAM; SSF48239; SSF48239; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..784
FT                   /note="Ent-kaurene synthase 2, chloroplastic"
FT                   /id="PRO_0000452390"
FT   MOTIF           528..532
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         528
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         528
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         532
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         532
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         672
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         680
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   784 AA;  89401 MW;  284BD3972DC09051 CRC64;
     MNLSLCIASP LLTKSNRPAA LSAIHTASTS HGGQTNPTNL IIDTTKERIQ KQFKNVEISV
     SSYDTAWVAM VPSPNSPKSP CFPECLNWLI NNQLNDGSWG LVNHTHNHNH PLLKDSLSST
     LACIVALKRW NVGEDQINKG LSFIESNLAS ATEKSQPSPI GFDIIFPGLL EYAKNLDINL
     LSKQTDFSLM LHKRELEQKR CHSNEMDGYL AYISEGLGNL YDWNMVKKYQ MKNGSVFNSP
     SATAAAFINH QNPGCLNYLN SLLDKFGNAV PTVYPHDLFI RLSMVDTIER LGISHHFRVE
     IKNVLDETYR CWVERDEQIF MDVVTCALAF RLLRINGYEV SPDPLAEITN ELALKDEYAA
     LETYHASHIL YQEDLSSGKQ ILKSADFLKE IISTDSNRLS KLIHKEVENA LKFPINTGLE
     RINTRRNIQL YNVDNTRILK TTYHSSNISN TDYLRLAVED FYTCQSIYRE ELKGLERWVV
     ENKLDQLKFA RQKTAYCYFS VAATLSSPEL SDARISWAKN GILTTVVDDF FDIGGTIDEL
     TNLIQCVEKW NVDVDKDCCS EHVRILFLAL KDAICWIGDE AFKWQARDVT SHVIQTWLEL
     MNSMLREAIW TRDAYVPTLN EYMENAYVSF ALGPIVKPAI YFVGPKLSEE IVESSEYHNL
     FKLMSTQGRL LNDIHSFKRE FKEGKLNAVA LHLSNGESGK VEEEVVEEMM MMIKNKRKEL
     MKLIFEENGS IVPRACKDAF WNMCHVLNFF YANDDGFTGN TILDTVKDII YNPLVLVNEN
     EEQR
 
 
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