KSL6_ORYSJ
ID KSL6_ORYSJ Reviewed; 821 AA.
AC A4KAG8; A0A0P0VKP2; Q0E083; Q2PHF1; Q69DS6; Q6Z5J0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ent-isokaur-15-ene synthase {ECO:0000305};
DE EC=4.2.3.103 {ECO:0000269|PubMed:16861806, ECO:0000269|PubMed:17456599};
DE AltName: Full=Ent-kaurene synthase-like 5 {ECO:0000303|PubMed:16861806};
DE Short=OsKS5 {ECO:0000303|PubMed:16861806};
DE AltName: Full=Ent-kaurene synthase-like 6 {ECO:0000303|PubMed:17456599};
DE Short=OsKS6 {ECO:0000303|PubMed:17456599};
DE Short=OsKSL6 {ECO:0000303|PubMed:17456599};
DE AltName: Full=Iso-kaurene synthase {ECO:0000305};
GN Name=KSL6 {ECO:0000303|PubMed:17456599};
GN Synonyms=KS5 {ECO:0000303|PubMed:16861806};
GN OrderedLocusNames=Os02g0571800 {ECO:0000305}, LOC_Os02g36264 {ECO:0000305};
GN ORFNames=P0689H05.34 {ECO:0000312|EMBL:BAD17276.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=17141283; DOI=10.1016/j.phytochem.2006.10.016;
RA Xu M., Wilderman P.R., Morrone D., Xu J., Roy A., Margis-Pinheiro M.,
RA Upadhyaya N.M., Coates R.M., Peters R.J.;
RT "Functional characterization of the rice kaurene synthase-like gene
RT family.";
RL Phytochemistry 68:312-326(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-624, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Nipponbare;
RX PubMed=15668792; DOI=10.1007/s00299-004-0896-6;
RA Margis-Pinheiro M., Zhou X.-R., Zhu Q.-H., Dennis E.S., Upadhyaya N.M.;
RT "Isolation and characterization of a Ds-tagged rice (Oryza sativa L.) GA-
RT responsive dwarf mutant defective in an early step of the gibberellin
RT biosynthesis pathway.";
RL Plant Cell Rep. 23:819-833(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-821, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16861806; DOI=10.1271/bbb.60044;
RA Kanno Y., Otomo K., Kenmoku H., Mitsuhashi W., Yamane H., Oikawa H.,
RA Toshima H., Matsuoka M., Sassa T., Toyomasu T.;
RT "Characterization of a rice gene family encoding type-A diterpene
RT cyclases.";
RL Biosci. Biotechnol. Biochem. 70:1702-1710(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ILE-664.
RX PubMed=17456599; DOI=10.1073/pnas.0611454104;
RA Xu M., Wilderman P.R., Peters R.J.;
RT "Following evolution's lead to a single residue switch for diterpene
RT synthase product outcome.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7397-7401(2007).
CC -!- FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids
CC natural products (PubMed:17456599, PubMed:16861806). Catalyzes the
CC conversion of ent-copalyl diphosphate to the phytoalexin precursor ent-
CC isokaur-15-ene (PubMed:17456599, PubMed:16861806).
CC {ECO:0000269|PubMed:16861806, ECO:0000269|PubMed:17456599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-isokaurene;
CC Xref=Rhea:RHEA:25759, ChEBI:CHEBI:33019, ChEBI:CHEBI:50783,
CC ChEBI:CHEBI:58553; EC=4.2.3.103;
CC Evidence={ECO:0000269|PubMed:16861806, ECO:0000269|PubMed:17456599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25760;
CC Evidence={ECO:0000269|PubMed:16861806, ECO:0000269|PubMed:17456599};
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:16861806, ECO:0000269|PubMed:17456599}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC {ECO:0000269|PubMed:15668792}.
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: Phytoalexins are diterpenoid secondary metabolites
CC involved in the defense mechanism of the plant and produced in response
CC to attack (by a pathogen, elicitor or UV irradiation).
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD17276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF09105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ823353; ABH10733.1; -; mRNA.
DR EMBL; AP005114; BAD17276.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF09105.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS79348.1; -; Genomic_DNA.
DR EMBL; AY347881; AAQ72564.1; -; mRNA.
DR EMBL; AB126936; BAE72101.1; -; mRNA.
DR RefSeq; XP_015625945.1; XM_015770459.1.
DR RefSeq; XP_015625947.1; XM_015770461.1.
DR AlphaFoldDB; A4KAG8; -.
DR SMR; A4KAG8; -.
DR STRING; 4530.OS02T0571800-00; -.
DR PaxDb; A4KAG8; -.
DR PRIDE; A4KAG8; -.
DR EnsemblPlants; Os02t0571800-00; Os02t0571800-00; Os02g0571800.
DR GeneID; 4329729; -.
DR Gramene; Os02t0571800-00; Os02t0571800-00; Os02g0571800.
DR KEGG; osa:4329729; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; A4KAG8; -.
DR OMA; MRTCAMA; -.
DR OrthoDB; 1658056at2759; -.
DR BioCyc; MetaCyc:MON-18623; -.
DR BRENDA; 4.2.3.103; 8948.
DR PlantReactome; R-OSA-9610720; Oryzalide A biosynthesis.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; A4KAG8; OS.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
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 Lyase; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT CHAIN 1..821
FT /note="Ent-isokaur-15-ene synthase"
FT /id="PRO_0000372319"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 556..560
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 560
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 560
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 701
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 705
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 664
FT /note="I->T: Changes catalytic activity. Converts ent-
FT copalyl diphosphate to ent-pimara-8(14),15-diene and
FT diphosphate."
FT /evidence="ECO:0000269|PubMed:17456599"
FT CONFLICT 92
FT /note="V -> A (in Ref. 6; BAE72101)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="L -> P (in Ref. 1; ABH10733 and 5; AAQ72564)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="R -> G (in Ref. 1; ABH10733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 92408 MW; 2191522B9B719A5D CRC64;
MMLPMSSACS GGQFPGASPH GIIPKQFSRA PRIRVSIRGA AGVEKSLGLG RNAGSQQGMH
KNELHDKIRK QLRDVQLQPS SYDTAWVAMV PVQGSHQTPR FPQSIEWILQ NQYDDGSWGT
NLPGLVVNKD ILLCTLACVV ALKRWNTGRD HISRGLNFIG RNFSVAMDEQ TVAPVGFNIT
FSGLLSLATR TGLELPVMQT DIDGIIHIRK IELERDAYGT ASSRRAFMAY VSEGLGNLQD
WNQVMAYQRK NGSIFNSPSA TAATIIHGHN YSGLAYLDFV TSKFGGPVPV MYPQNAYSQL
CMVDTLERMG ISESFACEIS DILDMTYRLW MHNEEELMLD MRTCAMAFRL LRMHGYDITS
DGMAQFVEQS SFDDSIHGYL NDTKALLELY KSSQLRCLED DLILEEIGSW SARVLLEKIS
SKMIHISELP EVEYALKCPV YAILERLEQK RNIEQFKTKE QLKIEGFKLL KSGYRGVIPN
DEILALAVDE FHSSQSVYQQ ELQDLNSWVA HTRLDELKFA RLMPSITYFS AAAVLLPSES
ARIAWTQNCI LTTTVDDFFD GEGSKEEMEN LVKLIEKWDD HGEIGFSSEC VEILFYAVYN
TSKQIAEKAM PLQKRNAVDH IAESWWFTVR GMLTEAEWRM DKYVPTTVEE YMSAAVDSFA
VGPIITSAAL FVGPELSEEV FRSEEYIHLM NLANTIGRLL NDMQTYEKEI KMGKVNSVML
HALSHSGGGR GSPEASMEEA KREMRRVLQG CRFELLRLVT RDAGVVPPPC RKLFWLMSKV
LHFVYMEKDR YFTAEGMMAS ANAVILDPLQ VTLPPSDSGT L
