KSL1_ISOJA
ID KSL1_ISOJA Reviewed; 797 AA.
AC A0A5P8DI06;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Ent-atiserene synthase KSL1, chloroplastic {ECO:0000305};
DE EC=4.2.3.185 {ECO:0000250|UniProtKB:A0A1Z3GBK8};
DE Flags: Precursor; Fragment;
GN Name=KSL1 {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 ent-copalyl diphosphate (ent-CPP) to ent-atiserene (By similarity).
CC {ECO:0000250|UniProtKB:A0A1Z3GBK8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-atiserene;
CC Xref=Rhea:RHEA:54496, ChEBI:CHEBI:33019, ChEBI:CHEBI:58553,
CC ChEBI:CHEBI:138219; EC=4.2.3.185;
CC Evidence={ECO:0000250|UniProtKB:A0A1Z3GBK8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54497;
CC Evidence={ECO:0000250|UniProtKB:A0A1Z3GBK8};
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:A0A1Z3GBK8}.
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; MK043035; QFP98579.1; -; mRNA.
DR AlphaFoldDB; A0A5P8DI06; -.
DR SMR; A0A5P8DI06; -.
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; 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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT <1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..797
FT /note="Ent-atiserene synthase KSL1, chloroplastic"
FT /id="PRO_0000452382"
FT REGION 21..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 547..551
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 21..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 551
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 551
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 691
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 699
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 797 AA; 90880 MW; 8B68C91AA6B98469 CRC64;
LVKDDMSLIL SSFSLFRSSR SSPASASLAG SGHPRTTPPK IASLQSPMVE ETKERIAKLF
KKKEVSRSTY DTAWVGMVPS PFSSEEPCFP DCLFWLLQNQ CPDGSWAQPH HHSLSPSLLN
KDVLSSTLAS ILALQKWGLG QRHIAKGLHF LELNFASATD NSQITPLGFD IVFPAMLDYA
ADLSLNLRLD PTTLNDLMNR RDSELKRCTE NGSAETEVYL AYIGEGMGKL HDWETVMKYQ
RKNGSLFNSP STTAAAFIAL GNSDCLKYLN SALKKFGSAV PAVYPLDIYS QLCIVDNLER
LGISRFFSTE IQSVLDDTYR CWLQGDEEIF MDASTCGLAF RTLRMNGYKV TSDSFIKVVQ
DCFSSSSPGH MRDVNTTLEL YRASELMLYP HEIELEKQNS RLRSLLEQEL SGGSIQSSQL
NAEVKQALDY PFYAVLDRMA KKKTIEHYNI DDSRILKTSF CLPSFGNKDL LSLSVQDYNR
CQAIHREELR EFDRWFVENR LDELEFARHK SAYYYCYFAA AATFFAPELS DARMSWAKNA
LMTTMVDDLF DVTGSVEEMK NLIQLVELWD VDVSTECRSH KVQILFSALK RTICEVGDRA
HQLQGRSIRS HIIVIWLDLL HSMMKEVEWS RDKFVPTMDE YVSNAYVSFA LGPIVLPALY
LVGPKLSEEM VNHSEYHNLF KLMSMCGRLL NDIRGYEREH DDGKLNAMSL YIMNNGGEIT
PEVAIMEIKS WNDRQRRELL RLVLEEKSVI PKACKDLFWH MCSVVHLFYN KDDGFWSQEL
IEVVNQVIHQ PILLSHF
