KSL1_SALMI
ID KSL1_SALMI Reviewed; 595 AA.
AC C8XPS0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Miltiradiene synthase KSL1, chloroplastic {ECO:0000305};
DE EC=4.2.3.131 {ECO:0000269|PubMed:19905026};
DE AltName: Full=Kaurene synthase-like 1 {ECO:0000303|PubMed:22291132};
DE Short=SmKSL {ECO:0000303|PubMed:19905026};
DE Short=SmKSL1 {ECO:0000303|PubMed:22291132};
DE Flags: Precursor;
GN Name=KSL1 {ECO:0000303|PubMed:22291132};
OS Salvia miltiorrhiza (Chinese sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=226208;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP JASMONATE.
RC TISSUE=Root hair;
RX PubMed=19905026; DOI=10.1021/ol902051v;
RA Gao W., Hillwig M.L., Huang L., Cui G., Wang X., Kong J., Yang B.,
RA Peters R.J.;
RT "A functional genomics approach to tanshinone biosynthesis provides
RT stereochemical insights.";
RL Org. Lett. 11:5170-5173(2009).
RN [2]
RP FUNCTION.
RX PubMed=21082262; DOI=10.1007/s11033-010-0383-9;
RA Cui G., Huang L., Tang X., Zhao J.;
RT "Candidate genes involved in tanshinone biosynthesis in hairy roots of
RT Salvia miltiorrhiza revealed by cDNA microarray.";
RL Mol. Biol. Rep. 38:2471-2478(2011).
RN [3]
RP INDUCTION BY JASMONATE.
RX PubMed=22291132; DOI=10.1093/jxb/err466;
RA Ma Y., Yuan L., Wu B., Li X., Chen S., Lu S.;
RT "Genome-wide identification and characterization of novel genes involved in
RT terpenoid biosynthesis in Salvia miltiorrhiza.";
RL J. Exp. Bot. 63:2809-2823(2012).
CC -!- FUNCTION: Involved in tanshinone biosynthesis in hairy roots
CC (PubMed:19905026, PubMed:21082262). Catalyzes the conversion of copalyl
CC diphosphate (CPP) to miltiradiene (PubMed:19905026, PubMed:21082262).
CC {ECO:0000269|PubMed:19905026, ECO:0000269|PubMed:21082262}.
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:19905026};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984;
CC Evidence={ECO:0000269|PubMed:19905026};
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Induced by jasmonate (MeJA) in roots.
CC {ECO:0000269|PubMed:19905026, ECO:0000269|PubMed:22291132}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF635966; ABV08817.1; -; mRNA.
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; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..595
FT /note="Miltiradiene synthase KSL1, chloroplastic"
FT /id="PRO_0000449931"
FT MOTIF 334..338
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 595 AA; 68370 MW; C6698501A8774CE9 CRC64;
MSLAFNPAAT AFSGNGARSR RENFPVKHVT VRGFPMITNK SSFAVKCNLT TTDLMGKIAE
KFKGEDSNFP AAAAVQPAAD MPSNLCIIDT LQRLGVDRYF RSEIDTILED TYRLWQRKER
AIFSDTAIHA MAFRLLRVKG YEVSSEELAP YADQEHVDLQ TIEVATVIEL YRAAQERTGE
DESSLKKLHA WTTTFLKQKL LTNSIPDKKL HKLVEYYLKN XHGILDRMGV RQNLDLYDIS
YYRTSKAANR FSNLCSEDFL AFARQDFNIC QAQHQKELQQ LQRWYADCKL DTLKYGRDVV
RVANFLTSAI IGDPELSDVR IVFAQHIVLV TRIDDFFDHR GSREESYKIL ELIKEWKEKP
AAEYGSEEVE ILFTAVYNTV NELAERAHVE QGRSVKDFLI KLWVQILSIF KRELDTWSDD
TALTLDDYLS ASWVSIGCRI CILMSMQFIG IKLSDEMLLS EECIDLCRHV SMVDRLLNDV
QTFEKERKEN TGNSVTLLLA ANKDDSSFTE EEAIRIAKEM AECNRRQLMQ IVYKTGTIFP
RQCKDMFLKV CRIGCYLYAS GDEFTSPQQM MEDMKSLVYE PLTIHPLVAN NVRGK
