KSL4_ORYSI
ID KSL4_ORYSI Reviewed; 840 AA.
AC Q66QH3; A2XQW6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=9-beta-pimara-7,15-diene synthase, chloroplastic {ECO:0000303|PubMed:15299118};
DE EC=4.2.3.35 {ECO:0000269|PubMed:15299118};
DE AltName: Full=Ent-kaurene synthase-like 4 {ECO:0000305};
DE Short=OsKS4 {ECO:0000305};
DE Short=OsKSL4 {ECO:0000305};
DE AltName: Full=OsDTS2 {ECO:0000303|PubMed:15299118};
DE AltName: Full=Syn-pimara-7,15-diene synthase {ECO:0000303|PubMed:15299118};
DE Flags: Precursor;
GN Name=KSL4 {ECO:0000305}; Synonyms=DTS2 {ECO:0000303|PubMed:15299118};
GN ORFNames=OsI_014459 {ECO:0000312|EMBL:AAU05906.1};
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], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=cv. IR24;
RX PubMed=15299118; DOI=10.1104/pp.104.045971;
RA Wilderman P.R., Xu M., Jin Y., Coates R.M., Peters R.J.;
RT "Identification of syn-pimara-7,15-diene synthase reveals functional
RT clustering of terpene synthases involved in rice phytoalexin/allelochemical
RT biosynthesis.";
RL Plant Physiol. 135:2098-2105(2004).
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: 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:15299118}.
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:15299118};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25561;
CC Evidence={ECO:0000269|PubMed:15299118};
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 -!- INDUCTION: Induced by methyl jasmonate (MeJa) and UV irradiation.
CC {ECO:0000269|PubMed:15299118}.
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: 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}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY616862; AAU05906.1; -; mRNA.
DR EMBL; CM000129; EEC76856.1; -; Genomic_DNA.
DR AlphaFoldDB; Q66QH3; -.
DR SMR; Q66QH3; -.
DR STRING; 39946.Q66QH3; -.
DR PRIDE; Q66QH3; -.
DR EnsemblPlants; BGIOSGA015980-TA; BGIOSGA015980-PA; BGIOSGA015980.
DR Gramene; BGIOSGA015980-TA; BGIOSGA015980-PA; BGIOSGA015980.
DR KEGG; ag:AAU05906; -.
DR HOGENOM; CLU_003125_2_0_1; -.
DR OMA; MNGYDIS; -.
DR BioCyc; MetaCyc:MON-6803; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034279; F:syn-pimara-7,15-diene 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 GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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..840
FT /note="9-beta-pimara-7,15-diene synthase, chloroplastic"
FT /id="PRO_0000372316"
FT MOTIF 589..593
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 733
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 737
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 741
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
SQ SEQUENCE 840 AA; 94758 MW; B0ECC89323C86A5E CRC64;
MASPMEAVAR SSLVLAPRRR RALGLLPAAA APFVLDCRRR HNGGMRRPHV SFACSAELDT
GRRQLPSTGT RAVMSSCPGY VEGRMVGENT SQINMGREAR IRRHLENPEF LPSSYDIAWV
AMVPLPGTDH LQAPCFPECV EWILQNQHSN GSWGVNEFDS SASKDILLST LACIIALEKW
NVGSEQIRRG LHFIAKNFSI VIDDQIAAPI GFNLTFPAMV NLAIKMGLEF PASEISIDQI
LHLRDMELKR LSGEESLGKE AYFAYIAEGL EESMVDWSEV MKFQGKNGSL FNSPAATAAA
LVHRYDDKAL GYLYSVVNKF GGEVPTVYPL NIFSQLSMVD TLVNIGISRH FSSDIKRILD
KTYILWSQRD EEVMLDLPTC AMAFRLLRMN GYGVSSDDLS HVAEASTFHN SVEGYLDDTK
SLLELYKASK VSLSENEPIL EKMGCWSGSL LKEKLCSDDI RGTPILGEVE YALKFPFYAT
LEPLDHKWNI ENFDARAYQK IKTKNMPCHV NEDLLALAAE DFSFCQSTYQ NEIQHLESWE
KENKLDQLEF TRKNLINSYL SAAATISPYE LSDARIACAK SIALTLVADD FFDVGSSKEE
QENLISLVEK WDQYHKVEFY SENVKAVFFA LYSTVNQLGA MASAVQNRDV TKYNVESWLD
YLRSLATDAE WQRSKYVPTM EEYMKNSIVT FALGPTILIA LYFMGQNLWE DIVKNAEYDE
LFRLMNTCGR LQNDIQSFER ECKDGKLNSV SLLVLDSKDV MSVEEAKEAI NESISSCRRE
LLRLVVREDG VIPKSCKEMF WNLYKTSHVF YSQADGFSSP KEMMGAMNGV IFEPLKTRGN
