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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

    Pathwayi: L-threonine biosynthesis

    This protein is involved in step 5 of the subpathway that synthesizes L-threonine from L-aspartate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. AK1 (AXX17_At5g12690), Aspartokinase 2, chloroplastic (AK2), Aspartokinase (AXX17_At5g13510), Aspartokinase 1, chloroplastic (AK1), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    4. Homoserine kinase (HSK)
    5. Threonine synthase 2, chloroplastic (TS2), Threonine synthase 1, chloroplastic (TS1)
    This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei172S-adenosyl-L-methionine 2; shared with dimeric partner1 Publication1
    Binding sitei173S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partner1 Publication1
    Binding sitei181S-adenosyl-L-methionine 3; in monomer B1 Publication1
    Binding sitei181S-adenosyl-L-methionine 4; in monomer A1 Publication1
    Binding sitei187S-adenosyl-L-methionine 3; in monomer B1 Publication1
    Binding sitei472Pyridoxal phosphateBy similarity1

    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
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G29840.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi205L → R in mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 40ChloroplastAdd BLAST40
    ChainiPRO_000003361741 – 526Threonine synthase 1, chloroplasticAdd BLAST486

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei203N6-(pyridoxal phosphate)lysine1

    Proteomic databases

    PaxDbiQ9S7B5.
    PRIDEiQ9S7B5.

    PTM databases

    iPTMnetiQ9S7B5.
    SwissPalmiQ9S7B5.

    Expressioni

    Gene expression databases

    GenevisibleiQ9S7B5. AT.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi14393. 1 interactor.
    STRINGi3702.AT4G29840.1.

    Structurei

    Secondary structure

    1526
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi60 – 64Combined sources5
    Beta strandi81 – 87Combined sources7
    Turni106 – 108Combined sources3
    Beta strandi110 – 115Combined sources6
    Helixi117 – 121Combined sources5
    Helixi125 – 133Combined sources9
    Turni134 – 137Combined sources4
    Turni141 – 144Combined sources4
    Helixi148 – 153Combined sources6
    Helixi160 – 162Combined sources3
    Beta strandi173 – 175Combined sources3
    Helixi177 – 184Combined sources8
    Beta strandi187 – 193Combined sources7
    Beta strandi196 – 201Combined sources6
    Helixi204 – 219Combined sources16
    Beta strandi226 – 229Combined sources4
    Helixi234 – 246Combined sources13
    Beta strandi250 – 255Combined sources6
    Helixi256 – 258Combined sources3
    Helixi261 – 269Combined sources9
    Beta strandi273 – 279Combined sources7
    Helixi281 – 294Combined sources14
    Beta strandi297 – 299Combined sources3
    Helixi300 – 302Combined sources3
    Helixi304 – 311Combined sources8
    Helixi313 – 321Combined sources9
    Turni322 – 324Combined sources3
    Beta strandi328 – 333Combined sources6
    Beta strandi335 – 337Combined sources3
    Helixi338 – 352Combined sources15
    Beta strandi355 – 357Combined sources3
    Beta strandi361 – 367Combined sources7
    Helixi368 – 370Combined sources3
    Helixi373 – 378Combined sources6
    Turni379 – 383Combined sources5
    Helixi395 – 397Combined sources3
    Helixi406 – 414Combined sources9
    Beta strandi418 – 422Combined sources5
    Helixi424 – 436Combined sources13
    Helixi443 – 457Combined sources15
    Beta strandi467 – 471Combined sources5
    Helixi475 – 478Combined sources4
    Helixi479 – 486Combined sources8
    Beta strandi502 – 506Combined sources5
    Helixi508 – 518Combined sources11

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9S7B5.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni142 – 144S-adenosyl-L-methionine 1 binding; shared with dimeric partner3
    Regioni165 – 167S-adenosyl-L-methionine 1 binding; shared with dimeric partner3
    Regioni335 – 339Pyridoxal phosphate bindingBy similarity5

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi159 – 162Poly-Asp4

    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

    eggNOGiENOG410IITN. Eukaryota.
    COG0498. LUCA.
    HOGENOMiHOG000076502.
    InParanoidiQ9S7B5.
    KOiK01733.
    OMAiKAKEANC.
    OrthoDBiEOG0936061W.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti2A → L in AAB04607 (PubMed:8706836).Curated1

    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.
    GrameneiAT4G29840.1; AT4G29840.1; AT4G29840.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1E5XX-ray2.25A/B41-526[»]
    2C2BX-ray2.60A/B/C/D/E/F41-526[»]
    2C2GX-ray2.61A/B41-526[»]
    ProteinModelPortaliQ9S7B5.
    SMRiQ9S7B5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14393. 1 interactor.
    STRINGi3702.AT4G29840.1.

    PTM databases

    iPTMnetiQ9S7B5.
    SwissPalmiQ9S7B5.

    Proteomic databases

    PaxDbiQ9S7B5.
    PRIDEiQ9S7B5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G29840.1; AT4G29840.1; AT4G29840.
    GeneIDi829106.
    GrameneiAT4G29840.1; AT4G29840.1; AT4G29840.
    KEGGiath:AT4G29840.

    Organism-specific databases

    TAIRiAT4G29840.

    Phylogenomic databases

    eggNOGiENOG410IITN. Eukaryota.
    COG0498. LUCA.
    HOGENOMiHOG000076502.
    InParanoidiQ9S7B5.
    KOiK01733.
    OMAiKAKEANC.
    OrthoDBiEOG0936061W.
    PhylomeDBiQ9S7B5.

    Enzyme and pathway databases

    UniPathwayiUPA00050; UER00065.
    BRENDAi4.2.3.1. 399.

    Miscellaneous databases

    EvolutionaryTraceiQ9S7B5.
    PROiQ9S7B5.

    Gene expression databases

    GenevisibleiQ9S7B5. AT.

    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...

    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: November 30, 2016
    This is version 134 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

    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 one 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.