KSL10_ORYSJ
ID KSL10_ORYSJ Reviewed; 815 AA.
AC Q2QQJ5; A0A0P0YAB2; Q00G36; Q60HB4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ent-sandaracopimara-8(14),15-diene synthase, chloroplastic {ECO:0000303|PubMed:15388982};
DE EC=4.2.3.29 {ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:21323642};
DE AltName: Full=Ent-kaurene synthase-like 10 {ECO:0000303|PubMed:16956633};
DE Short=OsKSL10 {ECO:0000303|PubMed:16956633};
DE AltName: Full=Ent-sandaracopimaradiene synthase {ECO:0000303|PubMed:15388982};
DE AltName: Full=Labdatriene synthase {ECO:0000303|PubMed:21323642};
DE EC=4.2.3.99 {ECO:0000269|PubMed:21323642};
DE Flags: Precursor;
GN Name=KSL10 {ECO:0000303|PubMed:16956633};
GN Synonyms=KS10 {ECO:0000303|PubMed:15388982};
GN OrderedLocusNames=Os12g0491800 {ECO:0000312|EMBL:BAT17204.1},
GN LOC_Os12g30824 {ECO:0000312|EMBL:ABA98308.2};
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].
RC STRAIN=cv. Nipponbare;
RX PubMed=16956633; DOI=10.1016/j.phytochem.2006.08.009;
RA Peters R.J.;
RT "Uncovering the complex metabolic network underlying diterpenoid
RT phytoalexin biosynthesis in rice and other cereal crop plants.";
RL Phytochemistry 67:2307-2317(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-815, FUNCTION, CATALYTIC ACTIVITY, AND
RP 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 [7]
RP INDUCTION.
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 [8]
RP FUNCTION.
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21323642; DOI=10.1042/bj20101429;
RA Morrone D., Hillwig M.L., Mead M.E., Lowry L., Fulton D.B., Peters R.J.;
RT "Evident and latent plasticity across the rice diterpene synthase family
RT with potential implications for the evolution of diterpenoid metabolism in
RT the cereals.";
RL Biochem. J. 435:589-595(2011).
CC -!- FUNCTION: Involved in the biosynthesis of oryzalexin A-F phytoalexins.
CC Catalyzes the conversion of ent-copalyl diphosphate to the phytoalexin
CC precursor ent-sandaracopimaradiene. {ECO:0000269|PubMed:15388982,
CC ECO:0000269|PubMed:17141283, ECO:0000269|PubMed:21323642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-sandaracopimara-
CC 8(14),15-diene; Xref=Rhea:RHEA:25536, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:50061, ChEBI:CHEBI:58553; EC=4.2.3.29;
CC Evidence={ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:21323642};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25537;
CC Evidence={ECO:0000269|PubMed:15388982, ECO:0000269|PubMed:21323642};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9alpha-copalyl diphosphate = (12E)-9alpha-labda-8(17),12,14-
CC triene + diphosphate; Xref=Rhea:RHEA:32151, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58622, ChEBI:CHEBI:63707; EC=4.2.3.99;
CC Evidence={ECO:0000269|PubMed:21323642};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32152;
CC Evidence={ECO:0000269|PubMed:21323642};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for ent-copalyl diphosphate {ECO:0000269|PubMed:21323642};
CC KM=5 uM for 9alpha-copalyl diphosphate {ECO:0000269|PubMed:21323642};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Induced by UV irradiation. {ECO:0000269|PubMed:15388982,
CC ECO:0000269|PubMed:16861806}.
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: ent-sandaracopimaradiene is a precursor of the
CC phytoalexins oryzalexins A-F. Phytoalexins are diterpenoid secondary
CC metabolites involved in the defense mechanism of the plant and produced
CC in response to attack (by a pathogen, elicitor or UV irradiation).
CC {ECO:0000305|PubMed:16956633}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; DQ823355; ABH10735.1; -; mRNA.
DR EMBL; DP000011; ABA98308.2; -; Genomic_DNA.
DR EMBL; AP008218; BAF29818.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT17204.1; -; Genomic_DNA.
DR EMBL; AB126937; BAD54752.1; -; mRNA.
DR RefSeq; XP_015618915.1; XM_015763429.1.
DR AlphaFoldDB; Q2QQJ5; -.
DR SMR; Q2QQJ5; -.
DR STRING; 4530.OS12T0491800-01; -.
DR PaxDb; Q2QQJ5; -.
DR PRIDE; Q2QQJ5; -.
DR EnsemblPlants; Os12t0491800-01; Os12t0491800-01; Os12g0491800.
DR GeneID; 4352248; -.
DR Gramene; Os12t0491800-01; Os12t0491800-01; Os12g0491800.
DR KEGG; osa:4352248; -.
DR eggNOG; ENOG502QVGX; Eukaryota.
DR HOGENOM; CLU_003125_2_0_1; -.
DR InParanoid; Q2QQJ5; -.
DR OMA; IGTWSAK; -.
DR OrthoDB; 372122at2759; -.
DR BRENDA; 4.2.3.29; 4460.
DR BRENDA; 4.2.3.99; 4460.
DR PlantReactome; R-OSA-1119371; Oryzalexin A-F biosynthesis.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QQJ5; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0034280; F:ent-sandaracopimaradiene 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 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 Chloroplast; Lyase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..815
FT /note="Ent-sandaracopimara-8(14),15-diene synthase,
FT chloroplastic"
FT /id="PRO_0000372323"
FT MOTIF 550..554
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 696
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 700
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 704
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT CONFLICT 68
FT /note="K -> R (in Ref. 1; ABH10735)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="G -> C (in Ref. 6; BAD54752)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="I -> M (in Ref. 6; BAD54752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 815 AA; 91930 MW; F483899E55ACA15D CRC64;
MLPSSICSMG QIPRTSPHYY GMLPKQMSKG HPPMVTRAVG GVEKGEVGGN VRSLQVMHSK
ELQAKIRKQL QRVELSPSLY DTAWVAMVPE RSSSQAPCYP QCIEWILQNQ HDDGSWGINS
SSLSVNKDIL LSTLACVVAL KKWNAGSYHI KRGLNFVGRN FSVAMDVQNI APVGFNVTFS
GLITLASGMG LQLPVWQTDI DEIFHLRKIE LERDSGGTIS ARKAFMAYVA EGFGSLQDWD
QVMAYQRKNG SLFNSPSTTA AAAIHTFNDR TLNYLDSLTN KFGGPVPAMY PQNIYSQLCT
VDALERTGIS QKFAREIRDI LDTTYRSWLH NEEEVMLDIP TCAMAFRLLR THGYDITSDE
MAHFSEQSSF DDSIHGYLND TKTLLELFKT SQIRFSCEDL VLENIGTWSA KLLKQQLLSN
KLSTSAQSEV EYVLKFPLHS TLDRLEHRRN IEQFKVEGSK VLKSGYCGSH SNEEILALAV
DYFHSSQSVY QQELKYFESW VKQCRLDELK FARVMPLIVH FSSAATIFAP ELADARMVLS
QTCMLITVYD DFFDCPEISR EEKENYIALI EKWDNHAEIG FCSKNVEIVF YAVYNTYKQI
GEKAALKQNR SIMDQLVEDL VSSAKAMMVE ADWTATKYIP ATMEEYMSNA EVSGAFASFV
CPPLYFLGLK LSEEDVKSHE YTQLLKLTNV IGRLQNDSQT YRKEILAGKV NSVLLRALTD
SGNTSPESIE AAKEIVNRDA ESSMVEMRSL VFSEGGPIPR PCKDRFWEMC KIVFYFYSED
DAYRTPKETM SSARAVILDP LRLIPPPSCP ETLSS
