KSB_SALMI
ID KSB_SALMI Reviewed; 806 AA.
AC A0A0U4CDK4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Ent-kaur-16-ene synthase, chloroplastic {ECO:0000305};
DE EC=4.2.3.19 {ECO:0000269|PubMed:26971881};
DE AltName: Full=Ent-kaurene synthase {ECO:0000303|PubMed:26971881};
DE Short=SmKS {ECO:0000303|PubMed:26971881};
DE Flags: Precursor;
GN Name=KS {ECO:0000303|PubMed:26971881};
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=26971881; DOI=10.1038/srep23057;
RA Su P., Tong Y., Cheng Q., Hu Y., Zhang M., Yang J., Teng Z., Gao W.,
RA Huang L.;
RT "Functional characterization of ent-copalyl diphosphate synthase, kaurene
RT synthase and kaurene oxidase in the Salvia miltiorrhiza gibberellin
RT biosynthetic pathway.";
RL Sci. Rep. 6:23057-23057(2016).
CC -!- FUNCTION: Catalyzes the conversion of ent-copalyl diphosphate to the
CC gibberellin precursor ent-kaur-16-ene. {ECO:0000269|PubMed:26971881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58553; EC=4.2.3.19;
CC Evidence={ECO:0000269|PubMed:26971881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
CC Evidence={ECO:0000269|PubMed:26971881};
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: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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; KT934790; ALX18649.1; -; mRNA.
DR AlphaFoldDB; A0A0U4CDK4; -.
DR SMR; A0A0U4CDK4; -.
DR BRENDA; 4.2.3.19; 9850.
DR UniPathway; UPA00390; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009899; F:ent-kaurene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..806
FT /note="Ent-kaur-16-ene synthase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449936"
FT MOTIF 545..549
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 549
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 549
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 689
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 697
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 806 AA; 92156 MW; 35D67A1DFFCA6AF5 CRC64;
MALPLSTCLL FHPKESRSRR FCFSPASASL KSGLHSATSA KIASMPTCFE QTRGRIAKLF
HKDELSVSTY DTAWVAMVPS PTSLEEPCFP DCLNWLLENQ CHDGSWARPH HHPLLKKDVL
SSTLACILAL KKWGVGEEQI KRGLHFLELN FASATDKCQI TPMGFDIIFP AMLDYARGFS
LNLRLDPTTF NDLMHKRDVE LKRSNRNYSS ETETYWAYIA EGMGELQNWE SVMKYQRRNG
SLFNCPSTTA AAFIALRNSD CLNYLHLALK KFGNAVSAVY PLDIYSQLCT VDNLERLGIS
QYFSTEIQNV LDETYRCWMQ GNEEIFMDAS TCALAFRTLR LNGYDVTSDP VTQILQECFS
SSFRGNMTDI NTTLELYRAS ELVLYPDERD LEKQNLRLKL LLEQELSSGL IQSCQLGRSI
NVEVNQAIEY PFYAIMDRVA KRKSIEHYNF DNTRILKTSY CSPNFSNEDF LFLSIEDFNR
CQAAHREELG ELERWVVENR LDELKFARSK SAYCYFSAAA TFFAPELLDA RLSWAKNGVL
TTVIDDFFDV GGSVEELKNL IQLVELWDVD ISTECYSHNV QIIFSALRRT ICEIGDKAFK
LQGRCITNHI IAIWLDLLNS MMRETEWARD NFVPTIDEYM SNAHVSFALG PIVLPALYLV
GPKLSEEMVN HSEYHNLFKL MSTCGRLLND IHGYERELKD GKLNALSLYI INHGGEVSKE
AAIWEMKSWI ETQRRELLRL VLEGKKSVLP KPCRELFWHM CSVVHLFYSK GDGFTSQDLI
QLVNTIIHQP ILLNDQTGAG LSKLHD
