KSL5_ORYSJ
ID KSL5_ORYSJ Reviewed; 821 AA.
AC Q6Z5J6; A0A0P0VKP5; Q2PHF2; Q69DS5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ent-pimara-8(14),15-diene synthase {ECO:0000305};
DE EC=4.2.3.30 {ECO:0000269|PubMed:16861806, ECO:0000269|PubMed:17456599};
DE AltName: Full=Ent-kaurene synthase-like 5 {ECO:0000303|PubMed:17456599};
DE Short=OsKS5 {ECO:0000303|PubMed:17456599};
DE Short=OsKSL5j {ECO:0000303|PubMed:17456599};
DE AltName: Full=Ent-kaurene synthase-like 6 {ECO:0000303|PubMed:16861806};
DE Short=OsKS6 {ECO:0000303|PubMed:16861806};
GN Name=KSL5 {ECO:0000303|PubMed:17456599};
GN Synonyms=KS6 {ECO:0000303|PubMed:16861806};
GN OrderedLocusNames=Os02g0571300 {ECO:0000305}, LOC_Os02g36220 {ECO:0000305};
GN ORFNames=P0689H05.20 {ECO:0000312|EMBL:BAD17270.1};
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], 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 [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 44-821, FUNCTION, CATALYTIC ACTIVITY, AND
RP 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 [6]
RP FUNCTION, MUTAGENESIS OF THR-664, CATALYTIC ACTIVITY, AND PATHWAY.
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:16861806, PubMed:17456599). Catalyzes the
CC conversion of ent-copalyl diphosphate to ent-pimara-8(14),15-diene
CC (PubMed:16861806, PubMed:17456599). {ECO:0000269|PubMed:16861806,
CC ECO:0000269|PubMed:17456599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-pimara-8(14),15-
CC diene; Xref=Rhea:RHEA:25540, ChEBI:CHEBI:33019, ChEBI:CHEBI:50063,
CC ChEBI:CHEBI:58553; EC=4.2.3.30;
CC Evidence={ECO:0000269|PubMed:16861806, ECO:0000269|PubMed:17456599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25541;
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: Highly expressed in roots, at intermediate levels
CC in stems and at lower levels in leaves. {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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AY347882; AAQ72565.1; -; mRNA.
DR EMBL; AP005114; BAD17270.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09104.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79346.1; -; Genomic_DNA.
DR EMBL; AB126935; BAE72100.1; -; mRNA.
DR RefSeq; XP_015625948.1; XM_015770462.1.
DR RefSeq; XP_015625949.1; XM_015770463.1.
DR AlphaFoldDB; Q6Z5J6; -.
DR SMR; Q6Z5J6; -.
DR STRING; 4530.OS02T0571300-01; -.
DR PaxDb; Q6Z5J6; -.
DR PRIDE; Q6Z5J6; -.
DR EnsemblPlants; Os02t0571300-01; Os02t0571300-01; Os02g0571300.
DR GeneID; 4329728; -.
DR Gramene; Os02t0571300-01; Os02t0571300-01; Os02g0571300.
DR KEGG; osa:4329728; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; Q6Z5J6; -.
DR OMA; RSKEYIH; -.
DR OrthoDB; 1659383at2759; -.
DR BioCyc; MetaCyc:MON-13866; -.
DR BRENDA; 4.2.3.30; 4460.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6Z5J6; OS.
DR GO; GO:0034282; F:ent-pimara-8(14),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 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT CHAIN 1..821
FT /note="Ent-pimara-8(14),15-diene synthase"
FT /id="PRO_0000372317"
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="T->I: Changes catalytic activity. Converts syn-
FT copalyl diphosphate to aphidicol-15-ene and diphosphate."
FT /evidence="ECO:0000269|PubMed:17456599"
FT CONFLICT 324
FT /note="I -> V (in Ref. 5; BAE72100)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="C -> R (in Ref. 1; AAQ72565)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="M -> V (in Ref. 1; AAQ72565)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="N -> D (in Ref. 5; BAE72100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 92377 MW; 52557D85FE875B11 CRC64;
MILPMSSACL GQFLRASPRG MIEQFNRAPP LRVSIRGAAG VEKSLGLGRN AGSQQGMQKN
QLQDKIRKQL REVQLSPSSY DTAWVAMVPV QGSHQTPRFP QCIEWILQNQ HDDGSWGTNL
PGSVVNKDIL LCTLACVVAL KRWNTGRDHI SRGLNFIGKN FWVAMDEQTI APVGFNITFS
GLLNLATGTG LEFPVMQTDI DGIFHMRKIE LERDAYGTAS SRRAFMAYVS EGLGSLQDWD
QVMAYQRKNR SIFNSPSAAA ATVIHGHNDS ALCYLDSLVS KLDGPVPVMY PQNAYSQLGM
VDTLEKMGIS NNFSCEISDI LDMIYRLWIH NEEELMLDMG TCAMAFRLLR MHGYDISSDG
MAQFVEQSSF DDSIHGYLND TKALLELYRS SQIRCLEDDL ILQDIGSWSA RVLQEKISSK
MTHKSEMLEV EYALKFPVYA TLERLEQKRN IEQFKTKEQL KIEGFKLLKS GYRGAITHDE
ILALAVDEFH SSQSVYQQEL QDLNSWVAQT RLDELKFARL MPSITYFSAA ATMFPSELSE
ARIAWTQNCI LTTTVDDFFD GDGSKEEMEN LVKLIEKWDG HGEIGFSSEC VEILFYAIYN
TSKQIAEKAV PLQKRNVVDH IAESWWFTVR GMLTEAEWRM DKYVPTTVEE YMSAAVDSFA
LGPTITSAAL FVGPELSEEV FRSKEYIHLM NLANTIGRLL NDMQTYEKEI KMGKVNSVML
HALSHSGGGR GSPEASMEEA KREMRRVLQG SRCDLLRLVT RDGGVVPPPC RKLFWFMSKV
LHFVYMEKDG YFTADGMMAS ANAVILDPLQ VTLLPSGLGT L
