ID   KSL1_ISOER              Reviewed;         776 AA.
AC   A0A3G1QTT3;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Ent-kaurene synthase-like 1 {ECO:0000303|PubMed:30496917};
DE            Short=IeKSL1 {ECO:0000303|PubMed:30496917};
DE            EC=4.2.3.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=KSL1 {ECO:0000303|PubMed:30496917};
OS   Isodon eriocalyx (Plectranthus eriocalyx).
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=662907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=30496917; DOI=10.1016/j.phytochem.2018.11.015;
RA   Du G., Gong H.-Y., Feng K.-N., Chen Q.-Q., Yang Y.-L., Fu X.-L., Lu S.,
RA   Zeng Y.;
RT   "Diterpene synthases facilitating production of the kaurane skeleton of
RT   eriocalyxin B in the medicinal plant Isodon eriocalyx.";
RL   Phytochemistry 158:96-102(2019).
CC   -!- FUNCTION: No detectable products in the presence of CPS2 or CPS3.
CC       {ECO:0000269|PubMed:30496917}.
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:0000250|UniProtKB:A0A1Z3GC64}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Barely detected in leaves and germinating seeds.
CC       {ECO:0000269|PubMed:30496917}.
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; KY937954; AWN06648.1; -; mRNA.
DR   AlphaFoldDB; A0A3G1QTT3; -.
DR   SMR; A0A3G1QTT3; -.
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:0042214; P:terpene metabolic process; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..776
FT                   /note="Ent-kaurene synthase-like 1"
FT                   /id="PRO_0000452393"
FT   MOTIF           522..526
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         522
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         522
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         526
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         526
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         666
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         674
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   776 AA;  89336 MW;  7E0B22A285CD356A CRC64;
     MFSLSLNLKT NPLLDNKTHR SSSGIGFRGS TISTVKCSLN NSKDLIVKIR ERVKGNVEIS
     PSAYDTAWVA MVPDREYSSQ RPRFPECLDW IVKNQNSDGS WGVQSPSMLK HSLSCTLACL
     LPLHKWNVAS PQLLRNGVEF IRSSALAATD KNQISPIGFD IIFPMMIQYA NDLNLELPLN
     QDLVHILFRN REAQLPRNKN LEYVAEGLGN SINWNKVLLM HQRSNGSLFN SPATTAAALI
     HRHDKKCLEY LNSLLSVYKT WVPTIHPVDV YARLCLVDHL QGLGVYRFFH PEIEDVLQET
     FRLWQQKDDE IFADTACRAM AFRLLRMQGY PVTPDALGAY VDGESFESSG TDTVLELYKA
     SQVRLPEDDD TLEKLHDWTF KFLKQQLESK TILDQQLLRK VEFNLKNHRG ILDAVKHRRN
     IDLYDIDHIR ILKTAYRFPT VYNEDIFLLS AQDFMTNQAQ FQKELQMLER WYYDDCRLDD
     MDFGRNVLRI THFISANMVY DPQLFEARLA FAKLISLTTR LDDFFDHHGS IQEAHLIIEL
     IREWNEPSTI TFPSQDVEIL YSAVYTTTTD LAEKAYPVQG RCIKSVLIYL WICILTGYKI
     EMASCTAETL PDIDEYIEIG QASIGVNICV LGFIHFLGVK ISEEMVMGEE CDKLWKNAAS
     ITRLLNDIQT FKKEQEERKI NSVIILMNSG LSEEEAVSNI LKMVIDKRKE LLKLVVRREG
     SVFPRIVRDA FRKTGNLGFY LYNFTDEFTL PLQMKEDMKL LFHDPPHVHS ATSHVT