KSL2_ISORU
ID KSL2_ISORU Reviewed; 752 AA.
AC A0A1X9ISP7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Kaurene synthase like 2, chloroplastic {ECO:0000303|PubMed:28381502};
DE EC=4.2.3.- {ECO:0000269|PubMed:28381502};
DE AltName: Full=Ent-isopimaradiene like synthase {ECO:0000305};
DE Flags: Precursor; Fragment;
GN Name=KSL2 {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 (PubMed:28381502). Catalyzes the conversion of
CC ent-copalyl diphosphate (ent-CPP) to ent-isopimaradiene like compounds
CC (PubMed:28381502). {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.
CC {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; KU180505; APJ36377.1; -; mRNA.
DR AlphaFoldDB; A0A1X9ISP7; -.
DR SMR; A0A1X9ISP7; -.
DR BRENDA; 4.2.3.B70; 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:0033331; P:ent-kaurene metabolic 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..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..>752
FT /note="Kaurene synthase like 2, chloroplastic"
FT /id="PRO_0000452391"
FT MOTIF 538..542
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 690
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT NON_TER 752
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 85257 MW; 99429F78518542F9 CRC64;
MSLLLSNSAL VGPKFRSSRI SHASASLDIG LQRATSPQNA SVATCFEETK GRIAKLFHKN
ELSVSTYDTA WVAMVPSPTS SEEPCFPACL NWLLENQCHD GSWARPHHHH MLKKDVLSST
LACILALKKW GVGEEQISRG LHFVELNFAS ATEKGQITPM GFDIIFPAML DNARGLSLNL
QLEPTTLNDL IYKRDLELKR CNQSNSAEKE VYWAHIAEGM GKLQDWESVM KYQRKNGSLF
NSPSTTAAAF IALRNSDCLN YLYSAMNKFG SAVPAVYPLD IYSQLCLVDN LERLGISRFF
STEIQSVLDD TYRCWLDGDE EIFMDASTCA LAFRTLRMNG YSVTSDSFTK AVQDCFSSSI
PSHMRDVNTT LELYRASEIM LYPDEIELEK QHSRLRSLLE HELSSGSIQS SQLNAVVKHA
LDYPFYAILD RMAKKKTIEH YEFDDTRILK TSFCSPTFGN KDFLSLSVED YNRCQAIHRK
EFRELDRWFK ETKLDELKFA RQKYTYSYCT AAASFASPEL SDARMSWAKN SVLIGIVDDL
FDVKGSVEEK QNLIKLVELW DVDVSTQCCS QSVQIIFSAL RSTICEIGDK GFKIQGRSIT
DHIIAIWLDV LYNMMKESEW AENKSVPTID EYMKISHVSS GLGPVVLPSL YLVGPKLSQE
MVNHSEYHSL FKLMSTCCRL LNDIRSYERE VEGGKPNALA LYRVSSGGEM MMSKEAAISE
LERLIERQRR ELMRTILEES VIPKCCKEIF GH
