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KSL5_ISORU
ID   KSL5_ISORU              Reviewed;         794 AA.
AC   A0A1Z3GC64;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Ent-kaurene synthase 5, chloroplastic {ECO:0000303|PubMed:28381502};
DE            Short=IrKSL5 {ECO:0000303|PubMed:28381502};
DE            EC=4.2.3.19 {ECO:0000269|PubMed:28381502};
DE   Flags: Precursor;
GN   Name=KSL5 {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, CATALYTIC ACTIVITY, PATHWAY, 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, and in the production of gibberellins
CC       phytohormones (PubMed:28381502). Catalyzes the conversion of ent-
CC       copalyl diphosphate (ent-CPP) to ent-kaurene (PubMed:28381502).
CC       {ECO:0000269|PubMed:28381502}.
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:28381502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
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   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous expression in roots, stems, leaves and
CC       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; KX580634; ASC55317.1; -; mRNA.
DR   AlphaFoldDB; A0A1Z3GC64; -.
DR   SMR; A0A1Z3GC64; -.
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:0033331; P:ent-kaurene metabolic 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..794
FT                   /note="Ent-kaurene synthase 5, chloroplastic"
FT                   /id="PRO_0000452387"
FT   MOTIF           543..547
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         543
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         543
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         547
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         547
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         687
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         695
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   794 AA;  90379 MW;  95026AA2CAAB6940 CRC64;
     MSLLLSNSAL VGPKFRSSRI SHASASLDIG LQRATSPQNA SVATCFEETK GRIAKLFHKN
     ELSVSTYDTA WVAMVPSPTS SEEPCFPACL NWLLENQCHD GSWARPHHHH MLKKDVLSST
     LACILALKKW GVGEEQINRG LHFVELNFAS ATEKGQITPM GFDIIFPAML DNARGLSLNL
     QLEPTTLNDL IYKRDLELKR CNQSNSAEKE VYWAHIAEGM GKLQDWESVM KYQRKNGSLF
     NCPSTTAAAF TALRNSDCLN YLRLALEKFG SAVPAVYPLD IYSQLCTVDN LERLGISRYF
     LTEIQSVLDE TYRSWLQGDE EIFMDASTCA LAFRTLRMNG YNVTSDPITK ILQECFSSSF
     RGNMTDINTT LEIYRASELI LYPEERDLDQ HNLRLKTFLE QELSSNGFIQ SCQLGRNINA
     EVNQAIEYPF YAIMDRMAKR KNIENYNIDN TRILKTSYRS PNFGNKDFLS LSVEDFNRCQ
     VIHREELREL ERWVIENRLD ELKFARSKAA YCYFSAAATI FSPELSDARM SWAKNGVLTT
     VVDDFFDVGG SVEELKNLIQ LVELWDVDVS TQCCSPNVQI IFSALKHTIC EIADKGFKLQ
     GRSITDHIIS IWLDLLYSMM KETELGIDKS FPTMDEYMSN AYVSFALGPI VLPALYLVGP
     KLSEEMVNHS EYHTLFKLMS TCGRLLNDIR GYERELKDGK ISAVSLYIMN NGGEITTEAA
     ISEMRSWIER DRRELLRLVL EENKSVLPKA CKKLFWHMCT VVHLFYRKDD GFTSLDLHGV
     VNAIINEPIV LNQF
 
 
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