KSL1_ISORU
ID KSL1_ISORU Reviewed; 626 AA.
AC A0A1W6QDI7; A0A1X9ISN1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Miltiradiene synthase KSL1, chloroplastic {ECO:0000303|PubMed:28445526};
DE EC=4.2.3.131 {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
DE AltName: Full=Kaurene synthase 1 {ECO:0000303|PubMed:28381502};
DE Short=IrKSL1 {ECO:0000303|PubMed:28381502};
DE AltName: Full=Terpene synthase 4 {ECO:0000303|PubMed:28445526};
DE Short=IrTPS4 {ECO:0000303|PubMed:28445526};
DE Flags: Precursor;
GN Name=KSL1 {ECO:0000303|PubMed:28381502};
GN Synonyms=TPS4 {ECO:0000303|PubMed:28445526};
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] (ISOFORM 2), FUNCTION, PATHWAY, CATALYTIC
RP ACTIVITY, AND 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PATHWAY, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=28445526; DOI=10.1371/journal.pone.0176507;
RA Pelot K.A., Hagelthorn L.M., Addison J.B., Zerbe P.;
RT "Biosynthesis of the oxygenated diterpene nezukol in the medicinal plant
RT Isodon rubescens is catalyzed by a pair of diterpene synthases.";
RL PLoS ONE 12:e0176507-e0176507(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, PubMed:28445526). Catalyzes
CC the conversion of (+)-copalyl diphosphate ((+)-CPP) to miltiradiene
CC (PubMed:28381502, PubMed:28445526). {ECO:0000269|PubMed:28381502,
CC ECO:0000269|PubMed:28445526}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene;
CC Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:65037; EC=4.2.3.131;
CC Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984;
CC Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
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, ECO:0000269|PubMed:28445526}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1W6QDI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1W6QDI7-2; Sequence=VSP_060991, VSP_060992;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, and, at low levels, in
CC stems and leaves. {ECO:0000269|PubMed:28381502,
CC ECO:0000269|PubMed:28445526}.
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; KU180504; APJ36376.1; -; mRNA.
DR EMBL; KX831652; ARO38142.1; -; mRNA.
DR AlphaFoldDB; A0A1W6QDI7; -.
DR SMR; A0A1W6QDI7; -.
DR BRENDA; 4.2.3.131; 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:0062205; F:miltiradiene synthase activity; IDA:UniProtKB.
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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Lyase; Magnesium; Metal-binding;
KW Plastid; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..626
FT /note="Miltiradiene synthase KSL1, chloroplastic"
FT /id="PRO_0000452385"
FT MOTIF 329..333
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT VAR_SEQ 592..597
FT /note="TELCQQ -> QSCVSN (in isoform 2)"
FT /id="VSP_060991"
FT VAR_SEQ 598..626
FT /note="Missing (in isoform 2)"
FT /id="VSP_060992"
FT CONFLICT 151
FT /note="H -> R (in Ref. 1; APJ36376)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="L -> M (in Ref. 1; APJ36376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 72049 MW; 9E49D6C54106B7B0 CRC64;
MSLAFNLRVI PFSGHTIQSR RGLFPVHESP MITTKPFAAV KCSLTTSTDL MGKIKEKFNG
KVHTSLPAIT THSADTPSNL CIIDTLQRLG VDRYFQSEID SILDDTYRLW QLKKEDIFSD
ITTHAMAFRL LRVKGYQVSS EELAPYADQE HVNLQEIDVP TVIELYRAAQ ERVTEEDSTL
KKLYVWTSTF LKQQLLTDAI PDKKLHEQVD YYLKNYHGIL DRMGVRRSLD LYDVGHYKTL
KAADGFSNLC NEDFLAFARQ DFNISQAQHQ KELQQLQRWY SDCRLDTLKF GRDVVRVSNF
LTSAMSGDPE LSDVRLAFAK HIVLVTRIDD FFDHGGSKEE SYKILELVKE WKEKPAGEYG
SEEVEILFTA VYNTVNELAE MAHIEQGRSV KDLLIKLWVE ILSMFKIELD TWSDDTALTL
DEYLSSSWVS IGCRICILIS MQFLGVKLTD EMLLSEECTD LCRHVSMVDR LLNDVQTFEK
ERKENTGNSV SLLLAAHKDE RAINEEEAIT KAKDLAEYNR RKLMQIVYKT GTIFPRKCKD
MFLKVCRIGC YLYSSGDEFT TPQQMMEDMK SLVYEPLTIH PPEANNVVGK KTELCQQLVK
PYVCHTFCKK YTVSRPSNVM MTCYID
