KSL7_ORYSJ
ID KSL7_ORYSJ Reviewed; 829 AA.
AC Q0E088; A0A0P0VKM2; Q6YV94; Q852S2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ent-cassa-12,15-diene synthase;
DE EC=4.2.3.28;
DE AltName: Full=Diterpene cyclase 1;
DE Short=OsDTC1;
DE AltName: Full=Ent-kaurene synthase-like 7;
DE Short=OsKSL7;
DE AltName: Full=OsKS3;
GN Name=KSL7; Synonyms=DTC1; OrderedLocusNames=Os02g0570400, LOC_Os02g36140;
GN ORFNames=OsJ_006992, OSJNBa0008E01.23;
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], FUNCTION, AND INDUCTION.
RX PubMed=14675427; DOI=10.1046/j.1365-313x.2003.01926.x;
RA Cho E.-M., Okada A., Kenmoku H., Otomo K., Toyomasu T., Mitsuhashi W.,
RA Sassa T., Yajima A., Yabuta G., Mori K., Oikawa H., Toshima H., Shibuya N.,
RA Nojiri H., Omori T., Nishiyama M., Yamane H.;
RT "Molecular cloning and characterization of a cDNA encoding ent-cassa-12,15-
RT diene synthase, a putative diterpenoid phytoalexin biosynthetic enzyme,
RT from suspension-cultured rice cells treated with a chitin elicitor.";
RL Plant J. 37:1-8(2004).
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
CC -!- FUNCTION: Involved in phytocassane phytoalexins biosynthesis. Catalyzes
CC the conversion of ent-copalyl diphosphate to the phytoalexin precursor
CC ent-cassa-12,15-diene. {ECO:0000269|PubMed:14675427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-cassa-12,15-diene;
CC Xref=Rhea:RHEA:25532, ChEBI:CHEBI:33019, ChEBI:CHEBI:50060,
CC ChEBI:CHEBI:58553; EC=4.2.3.28;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC {ECO:0000269|PubMed:15668792}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 2 to 6 days after imbibition.
CC {ECO:0000269|PubMed:15668792}.
CC -!- INDUCTION: By chitin oligosaccharide elicitor and UV irradiation.
CC {ECO:0000269|PubMed:14675427}.
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 -!- MISCELLANEOUS: Ent-cassa-12,15-diene is a precursor of the phytoalexins
CC phytocassanes A-E. 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=BAD17672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAZ23509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB089272; BAC56714.1; -; mRNA.
DR EMBL; AP005835; BAD17672.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008208; BAF09100.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79338.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ23509.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015622683.1; XM_015767197.1.
DR AlphaFoldDB; Q0E088; -.
DR SMR; Q0E088; -.
DR STRING; 4530.OS02T0570400-01; -.
DR PaxDb; Q0E088; -.
DR PRIDE; Q0E088; -.
DR EnsemblPlants; Os02t0570400-01; Os02t0570400-01; Os02g0570400.
DR GeneID; 4329724; -.
DR Gramene; Os02t0570400-01; Os02t0570400-01; Os02g0570400.
DR KEGG; osa:4329724; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; Q0E088; -.
DR OMA; HMKHERD; -.
DR OrthoDB; 318477at2759; -.
DR BioCyc; MetaCyc:DTC1-MON; -.
DR BRENDA; 4.2.3.28; 4460.
DR PlantReactome; R-OSA-1119583; Phytocassane biosynthesis.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q0E088; OS.
DR GO; GO:0034277; F:ent-cassa-12,15-diene synthase activity; IEA:UniProtKB-EC.
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 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 2: Evidence at transcript level;
KW Lyase; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT CHAIN 1..829
FT /note="Ent-cassa-12,15-diene synthase"
FT /id="PRO_0000372320"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 576..580
FT /note="DDXXD motif"
FT BINDING 576
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 576
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 728
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 436
FT /note="G -> GG (in Ref. 1; BAC56714)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="C -> S (in Ref. 1; BAC56714)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="E -> A (in Ref. 1; BAC56714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 829 AA; 92109 MW; 97F78B7C6229EEB8 CRC64;
MMLLGSPSSG GYGGKFAGAS PAGGTTTMAP SAKQPSSRAP PPGITGGRND LRILSPAAAA
AAVGGLEMKK PEAEGIAESL QATHRKELEA SIRKQLQGVE LSPSPYDTAW VAMVPLRGSS
HNPSFPQCVD WILENQWDDG SWSIDGSIST ANKDVLSSTL ACVLALNKWN VGREHIRRGL
SFIGRNFSIA MDDQAVAPIG FGITFPAMLT LANGSGLEVP VRQNDIDSLN HLREMKIQRE
AGNHSRGRKA YMAYLAEGFG NLLEWDEIMM FQRKNGSLFN CPSSTAGALA NYHDDKALQY
LQSLVNKFDG VVPTLYPLNI YCQLSMVDAL ENMGISQYFA SEIKSILDMT YSSWLGKDEE
IMLDVTTCAM AFRLLRMNGY DVSSDELSHV AGASGFRDSL QGYLNDRKSV LEVYKTSKHS
ISENDLILDS IGSWSGSLLK EMLCSNGKGT PGREEIEFAL KYPFYSTLER LVHRKNIVLF
DAKGSQMLKT ECMPVHDSQD FLALAVDDFC ISQSNYQNEL NYLESWVKDN RLDQLHFARQ
KITYCYLSGA ATTFRPEMGY ARTSWARTAW LTAVIDDLFD VGGLEQEQEN LLALMEKWEE
PGEDEYYSED VKIVFQALYN TVNEIGAKAS ALQGHDVTKY LVDVWLHVVR CMKVEAEWQR
SQHLPTFEEY MESGMVSLGQ GCTVMSALFL IGEKLPEGIV ELEEYDELFR LMGTCGRLLN
DIRGIEREES DGKMTNGVSL LVHASGGSMS VDEAKTEVMK RIDASRRKLL SLVVSEQEGP
IPRPCKQLFW KMCKILHLFY YQTDGFSSPK EMVSAVDAVI NEPLQLRLL
