ID   KSL4_ISORU              Reviewed;         806 AA.
AC   A0A1Z3GBK8;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Ent-atiserene synthase KSL4, chloroplastic {ECO:0000305};
DE            EC=4.2.3.185 {ECO:0000269|PubMed:28381502};
DE   AltName: Full=Kaurene synthase 4 {ECO:0000303|PubMed:28381502};
DE            Short=IrKSL4 {ECO:0000303|PubMed:28381502};
DE   Flags: Precursor;
GN   Name=KSL4 {ECO:0000303|PubMed:28381502};
OS   Isodon rubescens (Rabdosia rubescens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Isodoninae;
OC   Isodon.
OX   NCBI_TaxID=587669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=28381502; DOI=10.1104/pp.17.00202;
RA   Jin B., Cui G., Guo J., Tang J., Duan L., Lin H., Shen Y., Chen T.,
RA   Zhang H., Huang L.;
RT   "Functional diversification of kaurene synthase-like genes in Isodon
RT   rubescens.";
RL   Plant Physiol. 174:943-955(2017).
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 (PubMed:28381502). Catalyzes the conversion of
CC       ent-copalyl diphosphate (ent-CPP) to ent-atiserene (PubMed:28381502).
CC       {ECO:0000269|PubMed:28381502}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-copalyl diphosphate = diphosphate + ent-atiserene;
CC         Xref=Rhea:RHEA:54496, ChEBI:CHEBI:33019, ChEBI:CHEBI:58553,
CC         ChEBI:CHEBI:138219; EC=4.2.3.185;
CC         Evidence={ECO:0000269|PubMed:28381502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54497;
CC         Evidence={ECO:0000269|PubMed:28381502};
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:0000269|PubMed:28381502}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in leaves, and, at low levels, in
CC       roots, stems and flowers. {ECO:0000269|PubMed:28381502}.
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   -!- MISCELLANEOUS: Abietane diterpenoids (e.g. miltiradiene, abietatriene
CC       and ferruginol) accumulate specifically in the periderm of roots
CC       (PubMed:28381502). The ent-kaurene diterpenoid oridonin, main
CC       constituent of Isodon rubescens, accumulates in leaves
CC       (PubMed:28381502). {ECO:0000269|PubMed:28381502}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; KX580633; ASC55316.1; -; mRNA.
DR   AlphaFoldDB; A0A1Z3GBK8; -.
DR   SMR; A0A1Z3GBK8; -.
DR   KEGG; ag:ASC55316; -.
DR   BRENDA; 4.2.3.185; 15342.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:1901946; P:miltiradiene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
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; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..75
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           76..806
FT                   /note="Ent-atiserene synthase KSL4, chloroplastic"
FT                   /id="PRO_5012509352"
FT   REGION          33..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           556..560
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         556
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         556
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         560
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         560
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         700
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         708
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   806 AA;  91743 MW;  32A9F7B87E8EE325 CRC64;
     MGIVALILIK AAMSLILSSF PLFRSSRSSP ASASLAGSGL PKTTPPKTAS LQSHSPMFEE
     TKGRIAKLFK KNEVCISTYD TAWVGMVPSP FSSDQPCFPD SLFWLLDNQC PDGSWAQPHH
     HSHSHSPSLL NKDVLSSTLA SILALHKWGL GQHHIAKGLH FLELNFASAT DNSQITPLGF
     DIVFPAMLDH AADLSLNLRL DPTTLNDLMN RRDLELQRCT ENGSAETEVY MAYIGEGMGK
     LHDWESVMKY QRKNGSLFNS PSTTAAAFIA LRNSDCLNYL YSALNKFGSA VPAVYPLDIY
     SQLCIVDNLE RLGISRFFST EIQSVLDETY RCWLQGDEEI IMDASTCGLA FRTLRMNGYK
     VTSDSFIKVV QDCFSSPGHM RDVNTTLELY RASELMLYPH EIELEKQNSR LRSLLEQELS
     GGSIQSSQLN AEVKQALDYP FYAALDRMVK KKTIEHYNID DSRILKTSFR LPSFGNKDLL
     SLSVQDYNRC QAIHREELRE FDRWFVENRL DELEFARHKS AYYYCYFAAA ATFFAPELSD
     ARMSWAKNAL MTTMVDDLFD VTGSVEEMKN LIQLVELWDV DVSTECCSHK VQILFSALKR
     TICEVGDRAH QLQGRSIRSH IIVIWLDLLH SMMKEVEWTR DKFVPTMDEY VSNAHVSFAL
     GPIVLPALYL VGPKLSEEMV NHSEYHNLFK LMSMCGRLMN DIRGYEREHD DGKLNAMSLY
     IMNNGGEITP EVAILEIKSW NDRHRRDLLR LVLEEKSVIP KACKDLFWHM CSVVHLFYNK
     DDGFWSQELI EVVNQVIHQP ILLNHF