ID TPS03_ARATH Reviewed; 565 AA.
AC A4FVP2; O23517; Q84NE5; Q8GWA8; Q8LE37; Q9FVI5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Terpenoid synthase 3, chloroplastic {ECO:0000303|PubMed:12624761};
DE Short=AtTPS03 {ECO:0000303|PubMed:12624761};
DE AltName: Full=(E)-beta-ocimene synthase {ECO:0000303|PubMed:12624761, ECO:0000303|PubMed:20463089};
DE EC=4.2.3.106 {ECO:0000269|PubMed:12624761, ECO:0000269|PubMed:20463089};
DE AltName: Full=(E,E)-alpha-farnesene synthase {ECO:0000303|PubMed:20463089};
DE EC=4.2.3.46 {ECO:0000269|PubMed:20463089};
DE Flags: Precursor;
GN Name=TPS03 {ECO:0000303|PubMed:12624761};
GN OrderedLocusNames=At4g16740 {ECO:0000312|Araport:AT4G16740};
GN ORFNames=dl4395w {ECO:0000312|EMBL:CAB10449.1},
GN FCAALL.18 {ECO:0000312|EMBL:CAB78716.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-565 (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=cv. C24;
RX PubMed=12624761; DOI=10.1007/s00425-002-0924-0;
RA Faeldt J., Arimura G., Gershenzon J., Takabayashi J., Bohlmann J.;
RT "Functional identification of AtTPS03 as (E)-beta-ocimene synthase: a
RT monoterpene synthase catalyzing jasmonate- and wound-induced volatile
RT formation in Arabidopsis thaliana.";
RL Planta 216:745-751(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 163-292 (ISOFORMS 1/2).
RA Bohlmann J.;
RT "cDNA fragment of a monoterpene synthase AtTPS03 from Arabidopisis
RT thaliana.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INDUCTION BY HERBIVORY.
RX PubMed=11710601; DOI=10.1023/a:1012213116515;
RA Van Poecke R.M., Posthumus M.A., Dicke M.;
RT "Herbivore-induced volatile production by Arabidopsis thaliana leads to
RT attraction of the parasitoid Cotesia rubecula: chemical, behavioral, and
RT gene-expression analysis.";
RL J. Chem. Ecol. 27:1911-1928(2001).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA Aubourg S., Lecharny A., Bohlmann J.;
RT "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 267:730-745(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=12566586; DOI=10.1105/tpc.007989;
RA Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT flowers.";
RL Plant Cell 15:481-494(2003).
RN [12]
RP GENE FAMILY.
RX PubMed=12777052; DOI=10.1023/a:1023005504702;
RA Lange B.M., Ghassemian M.;
RT "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT in isoprenoid and chlorophyll metabolism.";
RL Plant Mol. Biol. 51:925-948(2003).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=16297850; DOI=10.1016/j.abb.2005.09.019;
RA Ro D.-K., Ehlting J., Keeling C.I., Lin R., Mattheus N., Bohlmann J.;
RT "Microarray expression profiling and functional characterization of AtTPS
RT genes: duplicated Arabidopsis thaliana sesquiterpene synthase genes
RT At4g13280 and At4g13300 encode root-specific and wound-inducible (Z)-gamma-
RT bisabolene synthases.";
RL Arch. Biochem. Biophys. 448:104-116(2006).
RN [14]
RP INDUCTION BY WOUNDING.
RX PubMed=17905899; DOI=10.1105/tpc.106.049981;
RA Catala R., Ouyang J., Abreu I.A., Hu Y., Seo H., Zhang X., Chua N.H.;
RT "The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought
RT responses.";
RL Plant Cell 19:2952-2966(2007).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=20463089; DOI=10.1104/pp.110.154864;
RA Huang M., Abel C., Sohrabi R., Petri J., Haupt I., Cosimano J.,
RA Gershenzon J., Tholl D.;
RT "Variation of herbivore-induced volatile terpenes among Arabidopsis
RT ecotypes depends on allelic differences and subcellular targeting of two
RT terpene synthases, TPS02 and TPS03.";
RL Plant Physiol. 153:1293-1310(2010).
CC -!- FUNCTION: Predominantly involved in sesquiterpenes (C15) biosynthesis.
CC Using FPP as substrate, the major product is (E,E)-alpha-farnesene with
CC minor amounts of (Z,E)-alpha-farnesene and (E,E)-beta-farnesene. Using
CC GPP as substrate, could also be able in vitro to synthesize monoterpene
CC (C10) with (E)-beta-ocimene as the major product and with (Z)-beta-
CC ocimene and myrcene as minor products. {ECO:0000269|PubMed:12624761,
CC ECO:0000269|PubMed:20463089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
CC Evidence={ECO:0000269|PubMed:20463089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27422;
CC Evidence={ECO:0000269|PubMed:20463089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64280; EC=4.2.3.106;
CC Evidence={ECO:0000269|PubMed:12624761, ECO:0000269|PubMed:20463089};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
CC Evidence={ECO:0000269|PubMed:12624761, ECO:0000269|PubMed:20463089};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q84LB2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 uM for (2E)-geranyl diphosphate {ECO:0000269|PubMed:20463089};
CC KM=2.6 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:20463089};
CC Vmax=539 pmol/sec/mg enzyme with (2E)-geranyl diphosphate as
CC substrate {ECO:0000269|PubMed:20463089};
CC Vmax=69 pmol/sec/mg enzyme with (2E,6E)-farnesyl diphosphate as
CC substrate {ECO:0000269|PubMed:20463089};
CC Note=kcat is 3.5x10(-2) sec(-1) with (2E)-geranyl diphosphate as
CC substrate (PubMed:20463089). kcat is 4.5x10(-3) sec(-1) with (2E,6E)-
CC farnesyl diphosphate as substrate (PubMed:20463089).
CC {ECO:0000269|PubMed:20463089};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:20463089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20463089}. Plastid,
CC chloroplast stroma {ECO:0000269|PubMed:20463089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A4FVP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4FVP2-2; Sequence=VSP_035151, VSP_035152;
CC Name=3;
CC IsoId=A4FVP2-3; Sequence=VSP_044001, VSP_044002;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers but also in
CC leaves, roots, stems and siliques. {ECO:0000269|PubMed:12566586,
CC ECO:0000269|PubMed:16297850}.
CC -!- INDUCTION: By coronalon, jasmonic acid and wounding, but not by
CC salicylic acid, cimene and limonene. Also induced in response to the
CC caterpillar P.xylostella or P.rapae feeding.
CC {ECO:0000269|PubMed:11710601, ECO:0000269|PubMed:12624761,
CC ECO:0000269|PubMed:17905899, ECO:0000269|PubMed:20463089}.
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:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- DISRUPTION PHENOTYPE: Reduction of TMTT, MeSA and (E,E)-alpha-farnesene
CC emmission. No formation of (E)-beta-ocimene detected.
CC {ECO:0000269|PubMed:20463089}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78716.1; Type=Erroneous gene model prediction; Evidence={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; Z97341; CAB10449.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161544; CAB78716.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83793.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83794.1; -; Genomic_DNA.
DR EMBL; AK118969; BAC43546.1; -; mRNA.
DR EMBL; BT030340; ABO38753.1; -; mRNA.
DR EMBL; AY085646; AAM62867.1; -; mRNA.
DR EMBL; AY151086; AAN65379.1; -; mRNA.
DR EMBL; AF180366; AAG09423.1; -; mRNA.
DR PIR; G71434; G71434.
DR RefSeq; NP_001031651.1; NM_001036574.1. [A4FVP2-2]
DR RefSeq; NP_567511.3; NM_117775.4. [A4FVP2-1]
DR AlphaFoldDB; A4FVP2; -.
DR SMR; A4FVP2; -.
DR STRING; 3702.A4FVP2; -.
DR PaxDb; 3702-AT4G16740-1; -.
DR ProteomicsDB; 232491; -. [A4FVP2-1]
DR EnsemblPlants; AT4G16740.1; AT4G16740.1; AT4G16740. [A4FVP2-1]
DR EnsemblPlants; AT4G16740.2; AT4G16740.2; AT4G16740. [A4FVP2-2]
DR GeneID; 827377; -.
DR Gramene; AT4G16740.1; AT4G16740.1; AT4G16740. [A4FVP2-1]
DR Gramene; AT4G16740.2; AT4G16740.2; AT4G16740. [A4FVP2-2]
DR KEGG; ath:AT4G16740; -.
DR Araport; AT4G16740; -.
DR TAIR; AT4G16740; TPS03.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR InParanoid; A4FVP2; -.
DR OMA; WKRMNEE; -.
DR OrthoDB; 1212461at2759; -.
DR PhylomeDB; A4FVP2; -.
DR BioCyc; ARA:AT4G16740-MONOMER; -.
DR BioCyc; MetaCyc:AT4G16740-MONOMER; -.
DR BRENDA; 4.2.3.106; 399.
DR BRENDA; 4.2.3.46; 399.
DR UniPathway; UPA00213; -.
DR PRO; PR:A4FVP2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A4FVP2; baseline and differential.
DR Genevisible; A4FVP2; AT.
DR GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:UniProtKB.
DR GO; GO:0052578; F:alpha-farnesene synthase activity; IMP:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IDA:TAIR.
DR GO; GO:0010333; F:terpene synthase activity; ISS:UniProtKB.
DR GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IMP:TAIR.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 1.
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 PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1.
DR PANTHER; PTHR31225:SF243; TERPENOID SYNTHASE 3, CHLOROPLASTIC; 1.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Cytoplasm; Lyase; Magnesium; Manganese;
KW Metal-binding; Plastid; Potassium; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 26..565
FT /note="Terpenoid synthase 3, chloroplastic"
FT /id="PRO_0000348422"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 320..324
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 283
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 320
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 324
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 458
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 474
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q84LB2"
FT VAR_SEQ 144
FT /note="D -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11910074, ECO:0000303|Ref.6"
FT /id="VSP_044001"
FT VAR_SEQ 145..565
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11910074, ECO:0000303|Ref.6"
FT /id="VSP_044002"
FT VAR_SEQ 388..396
FT /note="WADMCTTFL -> VRILIILSM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035151"
FT VAR_SEQ 397..565
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035152"
FT CONFLICT 27
FT /note="R -> L (in Ref. 6; AAM62867)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="N -> D (in Ref. 4; BAC43546)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> T (in Ref. 8; AAG09423)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="G -> S (in Ref. 8; AAG09423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 65753 MW; 126B4800002A2ECD CRC64;
MPKRQAQRRF TRKTDSKTPS QPLVSRRSAN YQPSLWQHEY LLSLGNTYVK EDNVERVTLL
KQEVSKMLNE TEGLLEQLEL IDTLQRLGVS YHFEQEIKKT LTNVHVKNVR AHKNRIDRNR
WGDLYATALE FRLLRQHGFS IAQDVFDGNI GVDLDDKDIK GILSLYEASY LSTRIDTKLK
ESIYYTTKRL RKFVEVNKNE TKSYTLRRMV IHALEMPYHR RVGRLEARWY IEVYGERHDM
NPILLELAKL DFNFVQAIHQ DELKSLSSWW SKTGLTKHLD FVRDRITEGY FSSVGVMYEP
EFAYHRQMLT KVFMLITTID DIYDIYGTLE ELQLFTTIVE KWDVNRLEEL PNYMKLCFLC
LVNEINQIGY FVLRDKGFNV IPYLKESWAD MCTTFLKEAK WYKSGYKPNF EEYMQNGWIS
SSVPTILLHL FCLLSDQTLD ILGSYNHSVV RSSATILRLA NDLATSSEEL ARGDTMKSVQ
CHMHETGASE AESRAYIQGI IGVAWDDLNM EKKSCRLHQG FLEAAANLGR VAQCVYQYGD
GHGCPDKAKT VNHVRSLLVH PLPLN
//
