KSL2_SALMI
ID KSL2_SALMI Reviewed; 811 AA.
AC H6VLG5; A0A0A7ANA5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Ent-13-epi-manoyl oxide synthase KSL2, chloroplastic {ECO:0000305};
DE EC=4.2.3.186 {ECO:0000269|PubMed:26077765};
DE AltName: Full=Kaurene synthase-like 2 {ECO:0000303|PubMed:22291132};
DE Short=SmKSL2 {ECO:0000303|PubMed:22291132};
DE Flags: Precursor;
GN Name=KSL2 {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, AND CATALYTIC ACTIVITY.
RX PubMed=26077765; DOI=10.1104/pp.15.00695;
RA Cui G., Duan L., Jin B., Qian J., Xue Z., Shen G., Snyder J.H., Song J.,
RA Chen S., Huang L., Peters R.J., Qi X.;
RT "Functional divergence of diterpene syntheses in the medicinal plant Salvia
RT miltiorrhiza.";
RL Plant Physiol. 169:1607-1618(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-811, AND 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 diterpenoid biosynthesis (PubMed:26077765).
CC Catalyzes the conversion of ent-8alpha-hydroxylabd-13-en-15-yl
CC diphospate to ent-13-epi-manoyl oxide (PubMed:26077765).
CC {ECO:0000269|PubMed:26077765}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-8alpha-hydroxylabd-13-en-15-yl diphosphate = diphosphate +
CC ent-13-epi-manoyl oxide; Xref=Rhea:RHEA:18721, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138223, ChEBI:CHEBI:138224; EC=4.2.3.186;
CC Evidence={ECO:0000269|PubMed:26077765};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18722;
CC Evidence={ECO:0000269|PubMed:26077765};
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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=AEZ55689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KC814643; AHJ59325.1; -; mRNA.
DR EMBL; JN831119; AEZ55689.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; H6VLG5; -.
DR SMR; H6VLG5; -.
DR KEGG; ag:AHJ59325; -.
DR BRENDA; 4.2.3.186; 14379.
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:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..811
FT /note="Ent-13-epi-manoyl oxide synthase KSL2,
FT chloroplastic"
FT /id="PRO_0000449932"
FT MOTIF 550..554
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 694
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 594
FT /note="R -> C (in Ref. 1; AHJ59325)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="D -> E (in Ref. 1; AHJ59325)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="D -> G (in Ref. 1; AHJ59325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 811 AA; 92639 MW; 50DFEC5AE912028B CRC64;
MALPLSTCLL FHPKESRSRR FCFSPASAAS LKSGLHSATS AKIASMPTCF EQTRGRIAKL
FHKDELSVST YDTAWVAMVP SPTSLEEPCF PDCLNWLLEN QCHDGSWARP HHHPLLKKDV
LSSTLACILA LKKWGVGEEQ IKRGLHFLEL NFASATDKCQ ITPMGFDIIF PAMLDYARGF
SLNLRLDPTT FNDLMHKRDL ELKRSNRNYS SETETYWAYI AEGMGELQNW ESVMKYQRRN
GSLFNCPSTT AAAFIALRNS DCLNYLHLAL KKFGNAVSAV YPLDIYSQLC TVDNLERLGI
SQYFSTEIQN VLDETYRCWM QGNEEIFMDA STCALAFRTL RLNGYDVTSD PVTKILQECF
SSSFRGNMTD INTTLELYRA SELVLYPDER DLEKQNLRLK LLLEQELSSG LIQSCQLGRS
INVLLISQVN QAIEYPFYAI MDRVAKRKSI EIYNFDNTRI LKTSYCSPNF GNEDFHFLSI
EDFNRCQAAH REELGELERW VVENRLDELK FARSKSAYCY FSAAATFFAP ELLDARLSWA
KNGVLTTVID DFFDVGGSVE ELKNLIQLVE LWDVDICTEC YSHNVQIIFS ALRRTICEIG
DKAFKLQGRC ITNHIIAIWL DLLNSMMRET EWARDNFVPT IDEYMSNAHV SFALGPIVLP
ALYLVGPKLS EDMVNHSEYH NLFKLMSTCG RLLNDIHGYE RELKDGKLNA LSLYIINHGG
EVSKEAAIWE MKSWIETQRR ELLRLVLEGK KSVLPKPCRE LFWHMCSVVH LFYSKGDGFT
SQDLIQLVNT IIHQPILLND QTGAGLSKLH D
