TPS5_SOLLC
ID TPS5_SOLLC Reviewed; 609 AA.
AC Q1XBU5; A0A3Q7ERH0;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=(R)-linalool synthase TPS5, chloroplastic {ECO:0000305};
DE EC=4.2.3.26 {ECO:0000269|PubMed:17440821};
DE AltName: Full=Monoterpene synthase 1 {ECO:0000303|PubMed:17440821};
DE Short=LeMTS1 {ECO:0000303|PubMed:17440821};
DE AltName: Full=Terpenoid synthase 5 {ECO:0000303|PubMed:21813655};
DE Flags: Precursor;
GN Name=TPS5 {ECO:0000303|PubMed:21813655};
GN Synonyms=MTS1 {ECO:0000303|PubMed:17440821};
GN OrderedLocusNames=Solyc01g105890 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION, AND DDXXD MOTIF.
RX PubMed=17440821; DOI=10.1007/s11103-007-9149-8;
RA van Schie C.C., Haring M.A., Schuurink R.C.;
RT "Tomato linalool synthase is induced in trichomes by jasmonic acid.";
RL Plant Mol. Biol. 64:251-263(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21813655; DOI=10.1104/pp.111.179648;
RA Falara V., Akhtar T.A., Nguyen T.T.H., Spyropoulou E.A., Bleeker P.M.,
RA Schauvinhold I., Matsuba Y., Bonini M.E., Schilmiller A.L., Last R.L.,
RA Schuurink R.C., Pichersky E.;
RT "The tomato terpene synthase gene family.";
RL Plant Physiol. 157:770-789(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Involved in monoterpene (C10) biosynthesis in glandular
CC trichomes (PubMed:17440821). Converts geranyl diphosphate to linalool
CC in glandular trichomes in response to jasmonate (JA) (PubMed:17440821).
CC Can convert farnesyl diphosphate to nerolidol in vitro
CC (PubMed:17440821). {ECO:0000269|PubMed:17440821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate;
CC Xref=Rhea:RHEA:15809, ChEBI:CHEBI:28, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.26;
CC Evidence={ECO:0000269|PubMed:17440821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (6E)-nerolidol +
CC diphosphate; Xref=Rhea:RHEA:56984, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:141283, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:17440821};
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 {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young fruits and plant tops
CC (PubMed:17440821). Expressed in flower buds and trichomes of petioles
CC and stems (PubMed:17440821). Expressed at low levels in young leaves,
CC stems, petioles, sepals and petals (PubMed:17440821).
CC {ECO:0000269|PubMed:17440821}.
CC -!- INDUCTION: Induced by spider mite feeding, wounding and jasmonate (JA).
CC {ECO:0000269|PubMed:17440821}.
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; AY840091; AAX69063.1; -; mRNA.
DR EMBL; JN408286; AEM05855.1; -; Genomic_DNA.
DR EMBL; CM001064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001233805.1; NM_001246876.3.
DR AlphaFoldDB; Q1XBU5; -.
DR SMR; Q1XBU5; -.
DR STRING; 4081.Solyc01g105890.2.1; -.
DR PaxDb; Q1XBU5; -.
DR PRIDE; Q1XBU5; -.
DR GeneID; 778246; -.
DR KEGG; sly:778246; -.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR InParanoid; Q1XBU5; -.
DR OrthoDB; 401091at2759; -.
DR PhylomeDB; Q1XBU5; -.
DR BioCyc; MetaCyc:MON2OL-32; -.
DR BRENDA; 4.2.3.26; 3101.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q1XBU5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034008; F:R-linalool synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
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; 2.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..609
FT /note="(R)-linalool synthase TPS5, chloroplastic"
FT /id="PRO_0000447554"
FT MOTIF 362..366
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:17440821"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 514
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 609 AA; 70945 MW; 3BEAB8BC9DF30082 CRC64;
MVSILSNIGM MVVTFKRPSL FTSLRRRSAN NIIITKHSHP ISTTRRSGNY KPTMWDFQFI
QSLHNPYEGD KYMKRLNKLK KEVKKMMMTV EGSHDEELEK LELIDNLERL GVSYHFKDEI
MQIMRSININ INIAPPDSLY TTALKFRLLR QHGFHISQDI LNDFKDENGN LKQSICKDTK
DILNSSKDEH DNLKQSTCNN TKGLLKLYEA SFLSIENESF LRNTTKSTLA HLMRYVDQNR
CGEEDNMIVE LVVHALELPR HWMVPRLETR WYISIYERMS NANPLLLELA KLDFNIVQAT
HQQDLRILSR WWKNTGLAEK LPFSRDILVE NMFWAVGALF EPQHSYFRRL ITKVIVFISI
IDDIYDVYGT LDELELFTLA IQRWDTKAME QLPDYMKVCY LALINIINEV AYEVLKNHDI
NVLPYLTKSW ADLCKSYLQE AKWYHNGYKP NLEEYMDNAR ISIGVPMVLV HSLFLVTNQI
TKEALDSLTN YPDIIRWSAT IFRLNDDLGT SSDELKRGDV SKSIQCYMNE KGASEEEAIE
HIEFLIQETW EAMNTAQSKN SPLSETFIEV AKNITKASHF MYLHSDVKSS ISKILFEPII
ISNVAFALK
