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Q9S7B5

- THRC1_ARATH

UniProt

Q9S7B5 - THRC1_ARATH

Protein

Threonine synthase 1, chloroplastic

Gene

TS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Pyridoxal phosphate.

    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

    Pathwayi

    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

    1. pyridoxal phosphate binding Source: InterPro
    2. threonine synthase activity Source: TAIR

    GO - Biological processi

    1. threonine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Threonine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    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: Chromosome 4

    Organism-specific databases

    TAIRiAT4G29840.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR
    3. cytosol Source: TAIR

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9S7B5.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi14393. 1 interaction.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01733.
    OMAiLAQAMFH.
    PhylomeDBiQ9S7B5.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [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

    MASSCLFNAS VSSLNPKQDP IRRHRSTSLL RHRPVVISCT ADGNNIKAPI    50
    ETAVKPPHRT EDNIRDEARR NRSNAVNPFS AKYVPFNAAP GSTESYSLDE 100
    IVYRSRSGGL LDVEHDMEAL KRFDGAYWRD LFDSRVGKST WPYGSGVWSK 150
    KEWVLPEIDD DDIVSAFEGN SNLFWAERFG KQFLGMNDLW VKHCGISHTG 200
    SFKDLGMTVL VSQVNRLRKM KRPVVGVGCA STGDTSAALS AYCASAGIPS 250
    IVFLPANKIS MAQLVQPIAN GAFVLSIDTD FDGCMKLIRE ITAELPIYLA 300
    NSLNSLRLEG QKTAAIEILQ QFDWQVPDWV IVPGGNLGNI YAFYKGFKMC 350
    QELGLVDRIP RMVCAQAANA NPLYLHYKSG WKDFKPMTAS TTFASAIQIG 400
    DPVSIDRAVY ALKKCNGIVE EATEEELMDA MAQADSTGMF ICPHTGVALT 450
    ALFKLRNQGV IAPTDRTVVV STAHGLKFTQ SKIDYHSNAI PDMACRFSNP 500
    PVDVKADFGA VMDVLKSYLG SNTLTS 526
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T08545.
    RefSeqi NP_194713.1. NM_119130.3.
    UniGenei At.23602.
    At.72983.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E5X X-ray 2.25 A/B 41-526 [» ]
    2C2B X-ray 2.60 A/B/C/D/E/F 41-526 [» ]
    2C2G X-ray 2.61 A/B 41-526 [» ]
    ProteinModelPortali Q9S7B5.
    SMRi Q9S7B5. Positions 76-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14393. 1 interaction.

    Proteomic databases

    PaxDbi Q9S7B5.
    PRIDEi Q9S7B5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G29840.1 ; AT4G29840.1 ; AT4G29840 .
    GeneIDi 829106.
    KEGGi ath:AT4G29840.

    Organism-specific databases

    TAIRi AT4G29840.

    Phylogenomic databases

    eggNOGi COG0498.
    HOGENOMi HOG000076502.
    KOi K01733.
    OMAi LAQAMFH.
    PhylomeDBi Q9S7B5.

    Enzyme and pathway databases

    UniPathwayi UPA00050 ; UER00065 .

    Miscellaneous databases

    EvolutionaryTracei Q9S7B5.

    Gene expression databases

    Genevestigatori Q9S7B5.

    Family and domain databases

    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR004450. Thr_synthase_like.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR00260. thrC. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 118 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