KSL4_ORYSJ
ID KSL4_ORYSJ Reviewed; 842 AA.
AC Q0JEZ8; A0A0N7KIL5; Q60HB5; Q69DS7; Q7XX63;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=9-beta-pimara-7,15-diene synthase, chloroplastic {ECO:0000303|PubMed:15388982};
DE EC=4.2.3.35 {ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:18366162};
DE AltName: Full=Ent-kaurene synthase-like 4 {ECO:0000303|PubMed:18366162};
DE Short=OsKS4 {ECO:0000303|PubMed:15388982};
DE Short=OsKSL4 {ECO:0000303|PubMed:18366162};
DE AltName: Full=OsDTS2 {ECO:0000305};
DE AltName: Full=Syn-pimara-7,15-diene synthase {ECO:0000303|PubMed:18366162};
DE Flags: Precursor;
GN Name=KSL4 {ECO:0000303|PubMed:18366162};
GN Synonyms=DTS2 {ECO:0000305}, KS4 {ECO:0000303|PubMed:15388982};
GN OrderedLocusNames=Os04g0179700, LOC_Os04g10060;
GN ORFNames=OsJ_013413, OSJNBa0052P16.14;
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, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=15388982; DOI=10.1271/bbb.68.2001;
RA Otomo K., Kanno Y., Motegi A., Kenmoku H., Yamane H., Mitsuhashi W.,
RA Oikawa H., Toshima H., Itoh H., Matsuoka M., Sassa T., Toyomasu T.;
RT "Diterpene cyclases responsible for the biosynthesis of phytoalexins,
RT momilactones A, B, and oryzalexins A-F in rice.";
RL Biosci. Biotechnol. Biochem. 68:2001-2006(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-698.
RX PubMed=18366162; DOI=10.1021/ja710524w;
RA Morrone D., Xu M., Fulton D.B., Determan M.K., Peters R.J.;
RT "Increasing complexity of a diterpene synthase reaction with a single
RT residue switch.";
RL J. Am. Chem. Soc. 130:5400-5401(2008).
CC -!- FUNCTION: Involved in the biosynthesis of momilactone A and B
CC phytoalexins. Catalyzes the conversion of syn-copalyl diphosphate to
CC the phytoalexin precursor syn-pimara-7,15-diene.
CC {ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:18366162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9alpha-copalyl diphosphate = 9beta-pimara-7,15-diene +
CC diphosphate; Xref=Rhea:RHEA:25560, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:50067, ChEBI:CHEBI:58622; EC=4.2.3.35;
CC Evidence={ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:18366162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25561;
CC Evidence={ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:18366162};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O81086};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:O81086};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:15668792}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 2 to 6 days after seed imbibition.
CC {ECO:0000269|PubMed:15668792}.
CC -!- INDUCTION: Induced by UV irradiation. {ECO:0000269|PubMed:15388982}.
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: 9-beta-pimara-7,15-diene is a precursor of the
CC phytoalexins momilactones A and B. Phytoalexins are diterpenoid
CC secondary metabolites involved in the defense mechanism of the plant
CC and produced in response to attack (by a pathogen, elicitor or UV
CC irradiation). Momilactone B can also act as an allochemical (an
CC antimicrobial and allelopathic agent), being constitutively produced in
CC the root of the plant and secreted to the rhizosphere where it
CC suppresses the growth of neighboring plants and soil microorganisms.
CC {ECO:0000305|PubMed:18366162}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD39717.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB126934; BAD54751.1; -; mRNA.
DR EMBL; AY347880; AAQ72563.1; -; mRNA.
DR EMBL; AL662936; CAD39717.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14089.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS87953.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE60594.1; -; Genomic_DNA.
DR RefSeq; XP_015633583.1; XM_015778097.1.
DR AlphaFoldDB; Q0JEZ8; -.
DR SMR; Q0JEZ8; -.
DR STRING; 4530.OS04T0179700-01; -.
DR PaxDb; Q0JEZ8; -.
DR PRIDE; Q0JEZ8; -.
DR EnsemblPlants; Os04t0179700-01; Os04t0179700-01; Os04g0179700.
DR GeneID; 4335094; -.
DR Gramene; Os04t0179700-01; Os04t0179700-01; Os04g0179700.
DR KEGG; osa:4335094; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; Q0JEZ8; -.
DR OMA; HDEVEFC; -.
DR OrthoDB; 318477at2759; -.
DR BRENDA; 4.2.3.35; 4460.
DR PlantReactome; R-OSA-1119308; Momilactone biosynthesis.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q0JEZ8; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0034279; F:syn-pimara-7,15-diene synthase activity; IEA:UniProtKB-EC.
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 Chloroplast; Lyase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..842
FT /note="9-beta-pimara-7,15-diene synthase, chloroplastic"
FT /id="PRO_0000372315"
FT MOTIF 591..595
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 591
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 591
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 735
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 739
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT MUTAGEN 698
FT /note="T->I: Changes catalytic activity. Converts syn-
FT copalyl diphosphate to aphidicol-15-ene and diphosphate."
FT /evidence="ECO:0000269|PubMed:18366162"
FT CONFLICT 145
FT /note="I -> M (in Ref. 2; AAQ72563)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> G (in Ref. 1; BAD54751)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="S -> G (in Ref. 1; BAD54751)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="N -> D (in Ref. 1; BAD54751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 842 AA; 94956 MW; B533670CF93D8835 CRC64;
MASPMEAVAR SSLVLAPRRR RALGLLPAAA AAAPFVLDCR RRHNGGMRRP HVSFACSAEL
DTGRRQLPST GTRAVMSSCP GYVEGRMVGE NTSQINMGWE ARILRHLENP EFLPSSYDIA
WVAMVPLPGT DHLQAPCFPE CVEWILQNQH SNGSWGVNEF DSSASKDILL STLACIIALE
KWNVGSEQIR RGLHFIAKNF SIVIDDQIAA PIGFNLTFPA MVNLAIKMGL EFPASEISID
QILHLRDMEL KRLAGDESLG KEAYFAYIAE GLEESMVDWS EVMKFQGKNG SLFNSPAATA
AALVHRYDDK ALGYLYSVVN KFGGEVPTVY PLNIFSQLSM VDTLVNIGIS RHFSSDIKRI
LDKTYILWSQ RDEEVMLDLP TCAMAFRLLR MNGYGVSSDD LSHVAEASTF HNSVEGYLDD
TKSLLELYKA SKVSLSENEP ILEKMGCWSG SLLKEKLCSD DIRGTPILRE VEYALKFPFY
ATLEPLDHKW NIENFDARAY QKIKTKNMPC HVNEDLLALA AEDFSFCQST YQNEIQHLES
WEKENKLDQL EFTRKNLINS YLSAAATISP YELSDARIAC AKSIALTLVA DDFFDVGSSK
EEQENLISLV EKWDQYHKVE FYSENVKAVF FALYSTVNQL GAMASAVQNR DVTKYNVESW
LDYLRSLATD AEWQRSKYVP TMEEYMKNSI VTFALGPTIL IALYFMGQNL WEDIVKNAEY
DELFRLMNTC GRLQNDIQSF ERECKDGKLN SVSLLVLDSK DVMSVEEAKE AINESISSCR
RELLRLVVRE DGVIPKSCKE MFWNLYKTSH VFYSQADGFS SPKEMMGAMN GVIFEPLKTR
GN
