LINS_ORYSJ
ID LINS_ORYSJ Reviewed; 595 AA.
AC Q6ZH94; A0A0N7KEL0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=S-(+)-linalool synthase, chloroplastic {ECO:0000305};
DE Short=OsLIS {ECO:0000303|PubMed:23889289};
DE EC=4.2.3.25 {ECO:0000305};
DE Flags: Precursor;
GN Name=LIS {ECO:0000303|PubMed:23889289};
GN OrderedLocusNames=Os02g0121700 {ECO:0000312|EMBL:BAF07634.1};
GN ORFNames=OJ1020_C02.21 {ECO:0000312|EMBL:BAD07605.1};
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].
RA Yuan J.S., Kollner T.G., Wiggins G., Grant J., Degenhardt J., Chen F.;
RT "Molecular and genomic basis of volatile-mediated indirect defense against
RT insects in rice.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY JASMONATE.
RX PubMed=23889289; DOI=10.1111/pce.12169;
RA Taniguchi S., Hosokawa-Shinonaga Y., Tamaoki D., Yamada S., Akimitsu K.,
RA Gomi K.;
RT "Jasmonate induction of the monoterpene linalool confers resistance to rice
RT bacterial blight and its biosynthesis is regulated by JAZ protein in
RT rice.";
RL Plant Cell Environ. 37:451-461(2014).
CC -!- FUNCTION: Involved in monoterpene (C10) biosynthesis. The major product
CC is S-(+)-linalool. Linalool production is induced by jasmonate in
CC response to pathogen attack, it possesses antibacterial activity and is
CC important for resistance to the bacterial blight pathogen Xanthomonas
CC oryzae pv. oryzae (Xoo). Plants over-expressing linalool synthase
CC display enhanced resistance to Xoo. {ECO:0000269|PubMed:23889289}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-linalool + diphosphate;
CC Xref=Rhea:RHEA:24116, ChEBI:CHEBI:98, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.25;
CC Evidence={ECO:0000305};
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:23889289}.
CC -!- INDUCTION: By jasmonate. {ECO:0000269|PubMed:23889289}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; EU596453; ACF05530.1; -; mRNA.
DR EMBL; AP004078; BAD07605.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07634.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76713.1; -; Genomic_DNA.
DR EMBL; AK110925; BAG99084.1; -; mRNA.
DR RefSeq; XP_015623808.1; XM_015768322.1.
DR AlphaFoldDB; Q6ZH94; -.
DR SMR; Q6ZH94; -.
DR STRING; 4530.OS02T0121700-01; -.
DR PaxDb; Q6ZH94; -.
DR PRIDE; Q6ZH94; -.
DR EnsemblPlants; Os02t0121700-01; Os02t0121700-01; Os02g0121700.
DR GeneID; 4328124; -.
DR Gramene; Os02t0121700-01; Os02t0121700-01; Os02g0121700.
DR KEGG; osa:4328124; -.
DR eggNOG; ENOG502QTGK; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR InParanoid; Q6ZH94; -.
DR OMA; VHLLFML; -.
DR OrthoDB; 449049at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034007; F:S-linalool synthase activity; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IDA:UniProtKB.
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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..595
FT /note="S-(+)-linalool synthase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_5004283133"
FT REGION 27..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 346..350
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 595 AA; 67266 MW; 7B49822FEB45FC00 CRC64;
MVCHVFSSFS SSLIRVLEAP LLLPAASASS SSSSSPASRS GGRRRRAAHV RPSPAIYPGR
QELASHSSML PTDFDIKVLI ERHEALTDDV QEMLQHQRRR HQKTASGGRE RIATVDHLRR
LCMDHYFQDE VDDAMDACLL EELAHGGDLL DATLAFRLMR EAGHHVSADE VLGRFTDDNG
EFRLDYRKDI RGLLSLQDIS HMNIGQEASL CKAKEFSTRN LESAINYLEP NLARYVRQSL
DHPYHVSLNQ YKARHHLSYL QTLPIRCTAM EELALADFQL NKLLHQMEMQ EIKRWWMDLG
LAQEIPVARD QVQKWFVWMM TAIQGASLSR CRIELTKIVS FVYIVDDIFD LVGTREELSC
FTQAIRMWDL AAADSLPSCM RSCFRALHTV TNDIADMVER EHGVNPINHL KKAWAMLFDG
FMTETKWLSA GQVPDSEEYL RNGVVTSGVP LVFVHLLFML GHDVSQNAAE FVDHIPPVIS
CPAKILRLWD DLGSAKDEAQ EGLDGSYKEL YLKENPGLAA GEAEEHVRRL IAGEWEELNR
ECFSASPSRS SPATTFPAGF TQAALNAARM VGVMYGYDGE RRLPVLDDYV RMLLF
