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TPS03_ARATH
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   03-AUG-2022, entry version 103.
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};
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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.AT4G16740.1; -.
DR   PaxDb; A4FVP2; -.
DR   PRIDE; A4FVP2; -.
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; locus:2129101; AT4G16740.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   HOGENOM; CLU_003125_7_1_1; -.
DR   InParanoid; A4FVP2; -.
DR   OMA; QECHPNI; -.
DR   OrthoDB; 401091at2759; -.
DR   PhylomeDB; A4FVP2; -.
DR   BioCyc; ARA:AT4G16740-MON; -.
DR   BioCyc; MetaCyc:AT4G16740-MON; -.
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; -; 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; 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   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 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         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="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         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
 
 
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