KSL2_ISOJA
ID KSL2_ISOJA Reviewed; 597 AA.
AC A0A5P8DI07;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Miltiradiene synthase KSL2, chloroplastic {ECO:0000303|Ref.1};
DE EC=4.2.3.131 {ECO:0000250|UniProtKB:A0A1W6QDI7};
DE AltName: Full=Kaurene synthase 2 {ECO:0000303|Ref.1};
DE Short=IjKSL2 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=KSL2 {ECO:0000303|Ref.1};
OS Isodon japonicus (Scutellaria japonica).
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=425908;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ide Y., Yamamura Y., Lee J.-B.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Catalyzes the conversion of
CC (+)-copalyl diphosphate ((+)-CPP) to miltiradiene (By similarity).
CC {ECO:0000250|UniProtKB:A0A1W6QDI7}.
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:0000250|UniProtKB:A0A1W6QDI7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984;
CC Evidence={ECO:0000250|UniProtKB:A0A1W6QDI7};
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:A0A1W6QDI7}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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; MK043036; QFP98580.1; -; mRNA.
DR AlphaFoldDB; A0A5P8DI07; -.
DR SMR; A0A5P8DI07; -.
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; ISS:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:1901946; P:miltiradiene biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; ISS: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 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..597
FT /note="Miltiradiene synthase KSL2, chloroplastic"
FT /id="PRO_0000452386"
FT MOTIF 329..333
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1W6QDI7"
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"
SQ SEQUENCE 597 AA; 68540 MW; 53034A6A969DEDEC CRC64;
MSLAFNLRAI PFSGHTIQSR RGLFPVHESP MITTKPFVAV KCSLTTSTDL MGKIKDKFNG
KVHTSLPAIT THSADTPCNL CIIDTLQRLG VDRYFQSEID SILDDTYRLW QLKKEDIFSD
ITTHAMAFRL LRVKGYQVSS EELAPYADQE RVNLQEIDVP TVIELYRAAQ ERVTEEDSTL
KKLYVWTSTF LKQQLLTDAI PDKKLHEQVD YYLKNYHGIL DRMGVRRSLD LYDVGHYKTL
KAADGFSNLC NEDLLAFAMQ DFNISQAQHQ KELQQLQRWY SDCRLDTLKF GRDVVRVSNF
LTSAMSGDPE LSDVRLAFAK HIVLVTRIDD FFDHGGSKEE SYKILELVKE WKEKPAGEYG
SEEIEILFTA VYNTVNELAE MAHIEQGRSV KDLLIKLWVE ILSIFKIELD TWSDDTALTL
DEYLSSSWVS IGCRICILIS MQFLGVKLTD EMLLSEECTD LCRHVSMVDR LLNDVQTFEK
ERKENTGNSV SLLLAAHKDE RAINEEEAIT KAKDLAEYNR RKLMQIVYKT GTIFPRKCKD
MFLKVCRIGC YLYSSGDEFT TPQQMMEDMK SLVYEPLTIH PPEANNVVGR KQSCVSN
