Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Threonine synthase 1, chloroplastic

Gene

TS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.

Catalytic activityi

O-phospho-L-homoserine + H2O = L-threonine + phosphate.

Cofactori

Enzyme regulationi

Allosterically activated by S-adenosyl-L-methionine (SAM). Activated by S-adenosyl-L-ethionine, 5'-amino-5'-deoxyadenosine, sinefungin and 5'-deoxy-5-methylthioadenosine. Inhibited by AMP.1 Publication

Kineticsi

  1. KM=30 µM for O-phospho-L-homoserine (in presence of 100 µM S-adenosyl-L-methionine)1 Publication
  2. KM=120 µM for O-phospho-L-homoserine (in absence of 100 µM S-adenosyl-L-methionine)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei172 – 1721S-adenosyl-L-methionine 2; shared with dimeric partner1 Publication
    Binding sitei173 – 1731S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partner1 Publication
    Binding sitei181 – 1811S-adenosyl-L-methionine 3; in monomer B1 Publication
    Binding sitei181 – 1811S-adenosyl-L-methionine 4; in monomer A1 Publication
    Binding sitei187 – 1871S-adenosyl-L-methionine 3; in monomer B1 Publication
    Binding sitei472 – 4721Pyridoxal phosphateBy similarity

    GO - Molecular functioni

    • pyridoxal phosphate binding Source: GO_Central
    • threonine synthase activity Source: TAIR

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi4.2.3.1. 399.
    UniPathwayiUPA00050; UER00065.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonine synthase 1, chloroplastic (EC:4.2.3.1)
    Alternative name(s):
    Protein METHIONINE OVER-ACCUMULATOR 2
    Gene namesi
    Name:TS1
    Synonyms:MTO2
    Ordered Locus Names:At4g29840
    ORF Names:F27B13.80
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G29840.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast stroma Source: TAIR
    • cytoplasm Source: GO_Central
    • cytosol Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi205 – 2051L → R in mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040ChloroplastAdd
    BLAST
    Chaini41 – 526486Threonine synthase 1, chloroplasticPRO_0000033617Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiQ9S7B5.
    PRIDEiQ9S7B5.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi14393. 1 interaction.
    STRINGi3702.AT4G29840.1.

    Structurei

    Secondary structure

    1
    526
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 645Combined sources
    Beta strandi81 – 877Combined sources
    Turni106 – 1083Combined sources
    Beta strandi110 – 1156Combined sources
    Helixi117 – 1215Combined sources
    Helixi125 – 1339Combined sources
    Turni134 – 1374Combined sources
    Turni141 – 1444Combined sources
    Helixi148 – 1536Combined sources
    Helixi160 – 1623Combined sources
    Beta strandi173 – 1753Combined sources
    Helixi177 – 1848Combined sources
    Beta strandi187 – 1937Combined sources
    Beta strandi196 – 2016Combined sources
    Helixi204 – 21916Combined sources
    Beta strandi226 – 2294Combined sources
    Helixi234 – 24613Combined sources
    Beta strandi250 – 2556Combined sources
    Helixi256 – 2583Combined sources
    Helixi261 – 2699Combined sources
    Beta strandi273 – 2797Combined sources
    Helixi281 – 29414Combined sources
    Beta strandi297 – 2993Combined sources
    Helixi300 – 3023Combined sources
    Helixi304 – 3118Combined sources
    Helixi313 – 3219Combined sources
    Turni322 – 3243Combined sources
    Beta strandi328 – 3336Combined sources
    Beta strandi335 – 3373Combined sources
    Helixi338 – 35215Combined sources
    Beta strandi355 – 3573Combined sources
    Beta strandi361 – 3677Combined sources
    Helixi368 – 3703Combined sources
    Helixi373 – 3786Combined sources
    Turni379 – 3835Combined sources
    Helixi395 – 3973Combined sources
    Helixi406 – 4149Combined sources
    Beta strandi418 – 4225Combined sources
    Helixi424 – 43613Combined sources
    Helixi443 – 45715Combined sources
    Beta strandi467 – 4715Combined sources
    Helixi475 – 4784Combined sources
    Helixi479 – 4868Combined sources
    Beta strandi502 – 5065Combined sources
    Helixi508 – 51811Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E5XX-ray2.25A/B41-526[»]
    2C2BX-ray2.60A/B/C/D/E/F41-526[»]
    2C2GX-ray2.61A/B41-526[»]
    ProteinModelPortaliQ9S7B5.
    SMRiQ9S7B5. Positions 76-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S7B5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 1443S-adenosyl-L-methionine 1 binding; shared with dimeric partner
    Regioni165 – 1673S-adenosyl-L-methionine 1 binding; shared with dimeric partner
    Regioni335 – 3395Pyridoxal phosphate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi159 – 1624Poly-Asp

    Domaini

    The N-terminal domain (1-77) is essential for regulation by S-adenosyl-L-methionine and AMP, but not for dimerization.

    Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000076502.
    InParanoidiQ9S7B5.
    KOiK01733.
    OMAiQSHHADP.
    PhylomeDBiQ9S7B5.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR00260. thrC. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9S7B5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASSCLFNAS VSSLNPKQDP IRRHRSTSLL RHRPVVISCT ADGNNIKAPI
    60 70 80 90 100
    ETAVKPPHRT EDNIRDEARR NRSNAVNPFS AKYVPFNAAP GSTESYSLDE
    110 120 130 140 150
    IVYRSRSGGL LDVEHDMEAL KRFDGAYWRD LFDSRVGKST WPYGSGVWSK
    160 170 180 190 200
    KEWVLPEIDD DDIVSAFEGN SNLFWAERFG KQFLGMNDLW VKHCGISHTG
    210 220 230 240 250
    SFKDLGMTVL VSQVNRLRKM KRPVVGVGCA STGDTSAALS AYCASAGIPS
    260 270 280 290 300
    IVFLPANKIS MAQLVQPIAN GAFVLSIDTD FDGCMKLIRE ITAELPIYLA
    310 320 330 340 350
    NSLNSLRLEG QKTAAIEILQ QFDWQVPDWV IVPGGNLGNI YAFYKGFKMC
    360 370 380 390 400
    QELGLVDRIP RMVCAQAANA NPLYLHYKSG WKDFKPMTAS TTFASAIQIG
    410 420 430 440 450
    DPVSIDRAVY ALKKCNGIVE EATEEELMDA MAQADSTGMF ICPHTGVALT
    460 470 480 490 500
    ALFKLRNQGV IAPTDRTVVV STAHGLKFTQ SKIDYHSNAI PDMACRFSNP
    510 520
    PVDVKADFGA VMDVLKSYLG SNTLTS
    Length:526
    Mass (Da):57,777
    Last modified:May 1, 2000 - v1
    Checksum:iB27787A57B882AD0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → L in AAB04607 (PubMed:8706836).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB027151 Genomic DNA. Translation: BAA77707.1.
    AL050352 Genomic DNA. Translation: CAB43659.1.
    AL161575 Genomic DNA. Translation: CAB79742.1.
    CP002687 Genomic DNA. Translation: AEE85684.1.
    L41666 mRNA. Translation: AAB04607.1.
    PIRiT08545.
    RefSeqiNP_194713.1. NM_119130.3.
    UniGeneiAt.23602.
    At.72983.

    Genome annotation databases

    EnsemblPlantsiAT4G29840.1; AT4G29840.1; AT4G29840.
    GeneIDi829106.
    KEGGiath:AT4G29840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB027151 Genomic DNA. Translation: BAA77707.1.
    AL050352 Genomic DNA. Translation: CAB43659.1.
    AL161575 Genomic DNA. Translation: CAB79742.1.
    CP002687 Genomic DNA. Translation: AEE85684.1.
    L41666 mRNA. Translation: AAB04607.1.
    PIRiT08545.
    RefSeqiNP_194713.1. NM_119130.3.
    UniGeneiAt.23602.
    At.72983.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E5XX-ray2.25A/B41-526[»]
    2C2BX-ray2.60A/B/C/D/E/F41-526[»]
    2C2GX-ray2.61A/B41-526[»]
    ProteinModelPortaliQ9S7B5.
    SMRiQ9S7B5. Positions 76-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14393. 1 interaction.
    STRINGi3702.AT4G29840.1.

    Proteomic databases

    PaxDbiQ9S7B5.
    PRIDEiQ9S7B5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G29840.1; AT4G29840.1; AT4G29840.
    GeneIDi829106.
    KEGGiath:AT4G29840.

    Organism-specific databases

    TAIRiAT4G29840.

    Phylogenomic databases

    eggNOGiCOG0498.
    HOGENOMiHOG000076502.
    InParanoidiQ9S7B5.
    KOiK01733.
    OMAiQSHHADP.
    PhylomeDBiQ9S7B5.

    Enzyme and pathway databases

    UniPathwayiUPA00050; UER00065.
    BRENDAi4.2.3.1. 399.

    Miscellaneous databases

    EvolutionaryTraceiQ9S7B5.
    PROiQ9S7B5.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR00260. thrC. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genomic nucleotide sequence of the Arabidopsis threonine synthase gene."
      Bartlem D., Tamaki Y., Naito S.
      Plant Gene Register PGR99-108
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Wassilewskija.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Characterization of an Arabidopsis thaliana cDNA encoding an S-adenosylmethionine-sensitive threonine synthase. Threonine synthase from higher plants."
      Curien G., Dumas R., Ravanel S., Douce R.
      FEBS Lett. 390:85-90(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-526, CHARACTERIZATION.
      Strain: cv. Columbia.
    5. "Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine."
      Curien G., Job D., Douce R., Dumas R.
      Biochemistry 37:13212-13221(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Characterization of recombinant Arabidopsis thaliana threonine synthase."
      Laber B., Maurer W., Hanke C., Graefe S., Ehlert S., Messerschmidt A., Clausen T.
      Eur. J. Biochem. 263:212-221(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, CRYSTALLIZATION.
    7. "Mutation in the threonine synthase gene results in an over-accumulation of soluble methionine in Arabidopsis."
      Bartlem D., Lambein I., Okamoto T., Itaya A., Uda Y., Kijima F., Tamaki Y., Nambara E., Naito S.
      Plant Physiol. 123:101-110(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-205.
    8. "Crystal structure of threonine synthase from Arabidopsis thaliana."
      Thomazeau K., Curien G., Dumas R., Biou V.
      Protein Sci. 10:638-648(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-526, PYRIDOXAL PHOSPHATE AT LYS-203.
    9. "Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site."
      Mas-Droux C., Biou V., Dumas R.
      J. Biol. Chem. 281:5188-5196(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 41-526 IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND S-ADENOSYL-L-METHIONINE.

    Entry informationi

    Entry nameiTHRC1_ARATH
    AccessioniPrimary (citable) accession number: Q9S7B5
    Secondary accession number(s): Q39144
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: May 1, 2000
    Last modified: June 24, 2015
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds 4 S-adenosyl-L-methionine (SAM) molecules per dimer. Although SAM3 and SAM4 have equivalent positions, their interactions with the protein are not identical. SAM3 interacts with Lys-181 and Asn-187 of monomer B, whereas SAM4 interacts only with Lys-181 of monomer A.
    Much more active than TS2 at physiological concentrations of S-adenosyl-L-methionine (20 µM).

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.