KSL11_ORYSI
ID KSL11_ORYSI Reviewed; 816 AA.
AC Q1AHB2; A2ZE63; B8BKG2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Stemod-13(17)-ene synthase;
DE EC=4.2.3.34;
DE AltName: Full=Ent-kaurene synthase-like 11;
DE Short=OsKSL11;
DE AltName: Full=Stemodene synthase;
GN Name=KSL11; Synonyms=KS11; ORFNames=OsI_034856, OsI_36076;
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], AND FUNCTION.
RX PubMed=16256063; DOI=10.1016/j.abb.2005.09.001;
RA Morrone D., Jin Y., Xu M., Choi S.-Y., Coates R.M., Peters R.J.;
RT "An unexpected diterpene cyclase from rice: functional identification of a
RT stemodene synthase.";
RL Arch. Biochem. Biophys. 448:133-140(2006).
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).
CC -!- FUNCTION: Catalyzes the conversion of syn-copalyl diphosphate to
CC stemodene. {ECO:0000269|PubMed:16256063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9alpha-copalyl diphosphate = diphosphate + stemod-13(17)-ene;
CC Xref=Rhea:RHEA:25556, ChEBI:CHEBI:33019, ChEBI:CHEBI:50068,
CC ChEBI:CHEBI:58622; EC=4.2.3.34;
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 -!- 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: Catalyzes the committed step in the biosynthesis of the
CC stemodane family of diterpenoid secondary metabolites, some of which
CC possess mild antiviral activity. Also produces stemod-12-ene and
CC stemar-13-ene as minor products.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:16256063, this sequence exists in both
CC japonica and indica subspecies and was submitted by the authors as a
CC japonica cultivar nipponbare sequence. However, the corresponding
CC sequence cannot be found in the currently available japonica nipponbare
CC genome or japonica expressed sequence tag data, but matches perfectly
CC in indica genome sequence. It is therefore annotated as indica
CC sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC68148.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ100373; AAZ76733.1; -; mRNA.
DR EMBL; CM000136; EEC68148.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q1AHB2; -.
DR SMR; Q1AHB2; -.
DR STRING; 39946.Q1AHB2; -.
DR KEGG; ag:AAZ76733; -.
DR HOGENOM; CLU_003125_2_0_1; -.
DR BioCyc; MetaCyc:MON-13868; -.
DR BRENDA; 4.2.3.34; 4460.
DR BRENDA; 4.2.3.B25; 4460.
DR Proteomes; UP000007015; Chromosome 11.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034283; F:syn-stemod-13(17)-ene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 Lyase; Magnesium; Metal-binding; Plant defense; Reference proteome.
FT CHAIN 1..816
FT /note="Stemod-13(17)-ene synthase"
FT /id="PRO_0000372324"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 553..557
FT /note="DDXXD motif"
FT BINDING 553
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 557
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 557
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 816 AA; 90385 MW; 3EB89DD3B7DF7C17 CRC64;
MMLLSSSYSG GQFPGVSPLG TRPKRSTTVV PLPVVTRATA GGVRNNLEVV GNAGTLQGMD
IDELRVIVRK QLQGVELSPS SYDTAWVAMV PVQGSPQSPC FPQCVEWILQ NQQEDGSWGH
SAGPSGEVNK DILLSTLACV LALNTWNVGQ DHIRRGLSFI GRNFSVAIDG QCAAPVGFNI
TFSGMLHLAI GMGLKFPVME TDIDSIFRLR EVEFERDAGG TASARKAFMA YVSEGLGREQ
DWDHVMAYQR KNGSLFNSPS TTAASAIHSC NDRALDYLVS LTSKLGGPVP AIHPDKVYSQ
LCMVDTLEKM GISSDFACDI RDILDMTYSC WMQDEEEIML DMATCAKAFR LLRMHGYDVS
SEGMARFAER SSFDDSIHAY LNDTKPLLEL YKSSQLHFLE EDLILENISS WSAKLLKQQL
SSNKIMKSLM PEVEYALKYP LYSTVDALEH RGNIERFNVN GFQRPKSGYC GSGADKEILA
LAVDKFHYNQ SVYQQELRYL ESWVAEFGLD ELKFARVIPL QSLLSALVPL FPAELSDARI
AFSQNCMLTT MVDDFFDGGG SMEEMVNFVA LIDEWDNHGE IGFCSNNVEI MFNAIYNTTK
RNCAKAALVQ NRCVMDHIAK QWQVMVRAMK TEAEWAASRH IPATMEEYMS VGEPSFALGP
IVPLSAYLLG EELPEEAVRS PEYGQLLRHA SAVGRLLNDV MTYEKEVLTW TPNSVLLQAL
AAARGGGESP TPPSPACAEA ARGEVRRAIQ ASWRDLHRLV FRDDDGSSIV PRACRELFWG
TAKVANVFYQ EVDGYTPKAM RGMANAVILD PLHLQQ
