KSL6_ISORU
ID KSL6_ISORU Reviewed; 775 AA.
AC A0A1Z3GCD1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Isopimaradiene synthase {ECO:0000305};
DE EC=4.2.3.- {ECO:0000269|PubMed:28381502};
DE AltName: Full=Kaurene synthase 6 {ECO:0000303|PubMed:28381502};
DE Short=IrKSL6 {ECO:0000303|PubMed:28381502};
DE Flags: Precursor;
GN Name=KSL6 {ECO:0000303|PubMed:28381502};
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], FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AND
RP 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).
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). Catalyzes the conversion of
CC (+)-copalyl diphosphate ((+)-CPP) to isopimaradiene (PubMed:28381502).
CC {ECO:0000269|PubMed:28381502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + isopimara-8(14),15-
CC diene; Xref=Rhea:RHEA:32003, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:63708; Evidence={ECO:0000269|PubMed:28381502};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32004;
CC Evidence={ECO:0000269|PubMed:28381502};
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}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in roots, stems, leaves and
CC flowers. {ECO:0000269|PubMed:28381502}.
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; KX580635; ASC55318.1; -; mRNA.
DR AlphaFoldDB; A0A1Z3GCD1; -.
DR SMR; A0A1Z3GCD1; -.
DR BRENDA; 4.2.3.44; 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: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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..775
FT /note="Isopimaradiene synthase"
FT /id="PRO_0000452381"
FT MOTIF 525..529
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 669
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 672
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 775 AA; 89113 MW; 2D82B860D8F9F3C7 CRC64;
MFSSSLKLKT NPLMDNKIHR SSSDRDFRGS TISSVKCSLN NSEDLIVKVR ERVKGKVEIS
PSAYDTAWVA MVPERDYSGQ KPRFPECLDW IVENQNADGS WGVQSSSMLK HSLSCTLACL
LPLRKWNVAS PQLLRNGVEF IRSSSSAATD KNQISPIGFD IVFPMMIQYA NDLNLELLLN
QDLVNILFQN REAQLTRNKN LEYVAEGLGS SIDWNKVLMH QRSNGSLFNS PATTAAALIH
RHDKKCLEYL NSLLSIYKTW VPTIHPMDVY ARLCLVDHLQ GLGVDRFVHP EIEVVLQETF
RLWQQKDDKI FTDATCRAMA FRLLRMQGYH VTPDELGGYV DEESFFATVS FESSGTDTVL
ELYKASQVRL PEDDDTLEKL HDWTSKFLKQ KLQSKTILDQ QLERKVEFNL KNYHGILDAV
KHRRNFDLYD IDHRRILKTA YRCPTVYNED ILLLTAQDLM TRQVQNQKEL QIMERWLEDC
RLDKVSGRNA VLVSYFLNAN NFPDPRLSEA RLAYAKTVTL ITFLDDFFDH HGSREDSLLI
MELINKWTEP LTVSYPSDEV EILYSALHAT ITDTAEKVYA VQGRCIKSLI IELWMEVLTA
MLGEMDSCNA DTPPDFDEYM AFAPKSLGCS LSILPSLHLM GETISEEMVT SLECFELDKH
VSIAIRLLND QQTFERERKE RTTNSVTLLM DADQISEEEA VSRIQKLIEH HTKELLKLVV
QKEGSVLPRK CKDIFWNTIK VGYCLYRFSD EFTSPQQMKE DMKLLFHDPV LKTTP
