Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 150 (18 Sep 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Threonine synthase 1, chloroplastic

Gene

TS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

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).

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphate

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Aspartokinase (AXX17_At3g01160), Aspartokinase 1, chloroplastic (AK1), Aspartokinase (CARAB-AK-LYS), Aspartokinase 3, chloroplastic (AK3), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    2. no protein annotated in this organism
    3. Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase, Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1)
    4. Homoserine kinase (HSK)
    5. Threonine synthase 1, chloroplastic (TS1), Threonine synthase 2, chloroplastic (TS2)
    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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAllosteric enzyme, Lyase
    Biological processAmino-acid biosynthesis, Threonine biosynthesis
    LigandPyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.3.1 399

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00050;UER00065

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Threonine synthase 1, chloroplastic (EC:4.2.3.1)
    Alternative name(s):
    Protein METHIONINE OVER-ACCUMULATOR 2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:TS1
    Synonyms:MTO2
    Ordered Locus Names:At4g29840
    ORF Names:F27B13.80
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT4G29840

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2123939 AT4G29840

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, Plastid

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi205L → R in mto2-1; causes a strong decrease in the concentration of soluble threonine and over-accumulation of methionine. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 40ChloroplastAdd BLAST40
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003361741 – 526Threonine synthase 1, chloroplasticAdd BLAST486

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei203N6-(pyridoxal phosphate)lysine1

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9S7B5

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9S7B5

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9S7B5

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q9S7B5

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9S7B5 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9S7B5 AT

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    14393, 9 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q9S7B5, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT4G29840.1

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1526
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9S7B5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q9S7B5

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi159 – 162Poly-Asp4

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the threonine synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IITN Eukaryota
    COG0498 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000076502

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9S7B5

    KEGG Orthology (KO)

    More...
    KOi
    K01733

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    VKIRGQG

    Database of Orthologous Groups

    More...
    OrthoDBi
    1361511at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9S7B5

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001926 PLP-dep
    IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
    IPR004450 Thr_synthase-like
    IPR036052 Trypto_synt_PLP_dependent

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00291 PALP, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53686 SSF53686, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00260 thrC, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00165 DEHYDRATASE_SER_THR, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB27787A57B882AD0
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2A → L in AAB04607 (PubMed:8706836).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T08545

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_194713.1, NM_119130.3

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT4G29840.1; AT4G29840.1; AT4G29840

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    829106

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT4G29840.1; AT4G29840.1; AT4G29840

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT4G29840

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    SMRiQ9S7B5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi14393, 9 interactors
    IntActiQ9S7B5, 1 interactor
    STRINGi3702.AT4G29840.1

    PTM databases

    iPTMnetiQ9S7B5
    SwissPalmiQ9S7B5

    Proteomic databases

    PaxDbiQ9S7B5
    PRIDEiQ9S7B5

    Genome annotation databases

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

    Organism-specific databases

    AraportiAT4G29840
    TAIRilocus:2123939 AT4G29840

    Phylogenomic databases

    eggNOGiENOG410IITN Eukaryota
    COG0498 LUCA
    HOGENOMiHOG000076502
    InParanoidiQ9S7B5
    KOiK01733
    OMAiVKIRGQG
    OrthoDBi1361511at2759
    PhylomeDBiQ9S7B5

    Enzyme and pathway databases

    UniPathwayiUPA00050;UER00065
    BRENDAi4.2.3.1 399

    Miscellaneous databases

    EvolutionaryTraceiQ9S7B5

    Protein Ontology

    More...
    PROi
    PR:Q9S7B5

    Gene expression databases

    ExpressionAtlasiQ9S7B5 baseline and differential
    GenevisibleiQ9S7B5 AT

    Family and domain databases

    InterProiView protein in InterPro
    IPR001926 PLP-dep
    IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
    IPR004450 Thr_synthase-like
    IPR036052 Trypto_synt_PLP_dependent
    PfamiView protein in Pfam
    PF00291 PALP, 1 hit
    SUPFAMiSSF53686 SSF53686, 1 hit
    TIGRFAMsiTIGR00260 thrC, 1 hit
    PROSITEiView protein in PROSITE
    PS00165 DEHYDRATASE_SER_THR, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTHRC1_ARATH
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9S7B5
    Secondary accession number(s): Q39144
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: May 1, 2000
    Last modified: September 18, 2019
    This is version 150 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again