KSL5_ORYSI
ID KSL5_ORYSI Reviewed; 821 AA.
AC A4KAG7; A2X6A6; B8AEA0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Ent-isokaur-15-ene synthase {ECO:0000305};
DE EC=4.2.3.103 {ECO:0000269|PubMed:17456599};
DE AltName: Full=Ent-kaurene synthase-like 5 {ECO:0000303|PubMed:17141283};
DE Short=OsKSL5i {ECO:0000303|PubMed:17141283};
DE AltName: Full=Isokaurene synthase {ECO:0000305};
GN Name=KSL5 {ECO:0000303|PubMed:17141283};
GN ORFNames=OsI_007599 {ECO:0000312|EMBL:EEC73447.1},
GN OsI_07744 {ECO:0000312|EMBL:EEC73447.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. IR24;
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. 93-11;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-661; ILE-664 AND
RP ILE-718.
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). Catalyzes the conversion of ent-
CC copalyl diphosphate to the phytoalexin precursor ent-isokaur-15-ene
CC (PubMed:17456599). {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:17456599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25760;
CC Evidence={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:17456599}.
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=EEC73447.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ823352; ABH10732.1; -; mRNA.
DR EMBL; CM000127; EEC73447.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A4KAG7; -.
DR SMR; A4KAG7; -.
DR STRING; 39946.A4KAG7; -.
DR PRIDE; A4KAG7; -.
DR KEGG; ag:ABH10732; -.
DR BioCyc; MetaCyc:MON-18622; -.
DR BRENDA; 4.2.3.103; 11590.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007015; Chromosome 2.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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_0000372318"
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 661
FT /note="V->L: No effect on the catalytic activity."
FT /evidence="ECO:0000269|PubMed:17456599"
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 MUTAGEN 718
FT /note="I->V: No effect on the catalytic activity."
FT /evidence="ECO:0000269|PubMed:17456599"
SQ SEQUENCE 821 AA; 92514 MW; AAF18A8F3E656023 CRC64;
MILPMSSACL GQFLRASPRG MIEQFNRAPP LRVSIRGAAG VEKSLGLGRN AGSQQGMQKN
QLQDKIRKQL REVQLSPSSY DTAWVAMVPV QGSHQTPRFP QCIEWIMQNQ HDDGSWGTNL
PGSVVNKDIL LCTLACVVAL KRWNTGRDHI SRGLNFIGKN FWVAMDEQTI APVGFNITFS
GLLNLATGTG LEFPVMQTDI DGIFHMRKIE LERDAYGTAS SRRAFMAYVS EGLDSLQDWD
QVMAYQRKNR SIFNSPSATA ATVIHGHNDS ALCYLDSLVS KLHGPVPVMY PQNAYSQLCM
VDTLEKMGIS NNFSCEISDI LDMIYRLWIH NEEELMLEMG TCAMAFRLLR MHGYDISSDG
MAQFVEQSSF DDSIHGYLND TKALLELYRS SQIRCLEDDL ILQDIGSWSA RVLQEKISSK
MTHKSEMLGV EYALKFPVYA TLERLEQKRN IEQFKTKEQL KIEGFKLLKS GYRGAITHDE
ILALAVDEFH SSQSVYQQEL QDLNSWVAHT RLDELKFARL MPSITYFSAA ATMFPSELSE
ARIAWTQNCI LTTTVDDFFD GDGSKEEMEN LVKLIKKWDG HGEIGFSSEC VEILFYAIYN
TSKQIAEKAV PLQKRNVVDH IAESWWFTVR GMLTEAEWRM DKYVPTTVEE YMSAAVDSFA
VGPIITSAAL FVGPELSEEV FRSEEYIHLM NLANTIGRLL NDMQTYEKEI KMGKVNSIML
HALSHSGGGR GSPEASMEEA KREMRRVLQG SRCDLLRLVT RDGGVVPPPC RKLFWFMSKV
LHFVYMEKDG YFTADGMMAS ANAVILDPLQ VTLLPSGLGT L
