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Entry version 32 (13 Nov 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Flavin-dependent thymidylate synthase

Gene

thyX

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH2 as the reductant (PubMed:18493582). Is essential for growth of the pathogen on solid media in vitro; the essential function is something other than dTMP synthase (PubMed:12657046) (PubMed:22034487).4 Publications

Miscellaneous

Was identified as a high-confidence drug target.1 Publication
Crystallographic studies have shown that NADPH/NADP+ binding expels both FAD and dUMP from the active site, by competing for the binding site (PubMed:16730023). However, the location of NADPH binding might not be biologically relevant (PubMed:18192395).1 Publication1 Publication

<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

FAD1 PublicationNote: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.1 Publication

<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

Is potently inhibited by 5-fluoro-2'-deoxyuridine 5'-monophosphate (FdUMP), but in contrast to ThyA, is not inhibited by the folate-based 1843U89 (PubMed:18493582). A 5-alkynyl dUMP analog has been shown to highly inhibit ThyX (IC50 value of 0.91 µM), while lacking activity against the classical mycobacterial thymidylate synthase ThyA, and therefore is a selective mycobacterial FDTS inhibitor (PubMed:21657202).2 Publications

<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

kcat is 0.4 min(-1).1 Publication
  1. KM=3 µM for dUMP1 Publication
  2. KM=4 µM for 5,10-methylenetetrahydrofolate1 Publication
  3. KM=47 µM for NADPH1 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: dTTP biosynthesis

    This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

    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 sitei71FAD; shared with neighboring subunitsCombined sources1 Publication1
    Binding sitei87dUMPCombined sources1 Publication1
    Binding sitei103FAD; via amide nitrogen and carbonyl oxygen; shared with neighboring subunitsCombined sources1 Publication1
    Binding sitei172dUMPCombined sources1 Publication1
    Binding sitei194FADCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei199Involved in ionization of N3 of dUMP, leading to its activationUniRule annotation1
    Binding sitei199dUMP; shared with dimeric partnerCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi92 – 95dUMP; shared with dimeric partnerCombined sources1 Publication4
    Nucleotide bindingi95 – 97FADCombined sources1 Publication3
    Nucleotide bindingi103 – 107dUMPCombined sources1 Publication5
    Nucleotide bindingi188 – 190FAD; shared with neighboring subunitsCombined sources1 Publication3

    <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

    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 functionMethyltransferase, Transferase
    Biological processNucleotide biosynthesis
    LigandFAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:G185E-7003-MONOMER
    MTBH37RV:G185E-7003-MONOMER

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

    More...
    UniPathwayi
    UPA00575

    <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:
    Flavin-dependent thymidylate synthase2 Publications (EC:2.1.1.1481 Publication)
    Short name:
    FDTS1 Publication
    Alternative name(s):
    FAD-dependent thymidylate synthase1 Publication
    Thymidylate synthase ThyX1 Publication
    Short name:
    TS1 Publication
    Short name:
    TSaseUniRule annotation
    <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:thyX1 Publication
    Ordered Locus Names:Rv2754c
    ORF Names:MTV002.19c
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv2754c

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene display impaired growth (PubMed:12657046). Strains with a thyX deletion could not be obtained (PubMed:22034487).2 Publications

    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>Mutagenesisi65I → M: Still able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi69H → E: Loss of catalytic activity since it is not able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi95R → A or D: Loss of catalytic activity since it is not able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi95R → K: Still able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi105S → E: Loss of catalytic activity since it is not able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi108Y → F: Still able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi165K → A: Loss of catalytic activity since it is not able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi168R → A: Loss of catalytic activity since it is not able to complement an E.coli thyA deletion mutant. 1 Publication1
    Mutagenesisi175L → M: Still able to complement an E.coli thyA deletion mutant. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1795161

    <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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001755701 – 250Flavin-dependent thymidylate synthaseAdd BLAST250

    Proteomic databases

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

    More...
    PaxDbi
    P9WG57

    <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

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Is expressed under the exponential phase of growth, and down-regulated upon starvation. Expression of thyX is significantly increased within murine macrophages or under acid stress. Is expressed at a lower level than thyA under all of the in vitro and in vivo growth conditions tested.1 Publication

    <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

    Homotetramer.

    3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv2754c

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P9WG57

    <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

    1250
    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
    P9WG57

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 233ThyXPROSITE-ProRule annotationAdd BLAST227

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi95 – 105ThyX motifUniRule annotationAdd BLAST11

    <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 thymidylate synthase ThyX family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107SMJ Bacteria
    COG1351 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K03465

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WAKLGPR

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WG57

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.70.3180, 2 hits

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01408 ThyX, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003669 Thymidylate_synthase_ThyX
    IPR036098 Thymidylate_synthase_ThyX_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR34934 PTHR34934, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02511 Thy1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF69796 SSF69796, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR02170 thyX, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51331 THYX, 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.

    P9WG57-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAETAPLRVQ LIAKTDFLAP PDVPWTTDAD GGPALVEFAG RACYQSWSKP
    60 70 80 90 100
    NPKTATNAGY LRHIIDVGHF SVLEHASVSF YITGISRSCT HELIRHRHFS
    110 120 130 140 150
    YSQLSQRYVP EKDSRVVVPP GMEDDADLRH ILTEAADAAR ATYSELLAKL
    160 170 180 190 200
    EAKFADQPNA ILRRKQARQA ARAVLPNATE TRIVVTGNYR AWRHFIAMRA
    210 220 230 240 250
    SEHADVEIRR LAIECLRQLA AVAPAVFADF EVTTLADGTE VATSPLATEA
    Length:250
    Mass (Da):27,591
    Last modified:April 16, 2014 - 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:i7BACFA59B5DA7294
    GO

    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
    AL123456 Genomic DNA Translation: CCP45553.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A70880

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_217270.1, NC_000962.3
    WP_003899465.1, NZ_NVQJ01000020.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP45553; CCP45553; Rv2754c

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    887766

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv2754c
    mtv:RVBD_2754c

    <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
    AL123456 Genomic DNA Translation: CCP45553.1
    PIRiA70880
    RefSeqiNP_217270.1, NC_000962.3
    WP_003899465.1, NZ_NVQJ01000020.1

    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
    2AF6X-ray2.01A/B/C/D/E/F/G/H1-250[»]
    2GQ2X-ray2.10A/B/C/D1-250[»]
    3GWCX-ray1.90A/B/C/D/E/F/G/H1-250[»]
    3HZGX-ray2.45A/B/C/D1-250[»]
    SMRiP9WG57
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2754c

    Chemistry databases

    BindingDBiP9WG57
    ChEMBLiCHEMBL1795161

    Proteomic databases

    PaxDbiP9WG57

    Genome annotation databases

    EnsemblBacteriaiCCP45553; CCP45553; Rv2754c
    GeneIDi887766
    KEGGimtu:Rv2754c
    mtv:RVBD_2754c

    Organism-specific databases

    TubercuListiRv2754c

    Phylogenomic databases

    eggNOGiENOG4107SMJ Bacteria
    COG1351 LUCA
    KOiK03465
    OMAiWAKLGPR
    PhylomeDBiP9WG57

    Enzyme and pathway databases

    UniPathwayiUPA00575
    BioCyciMetaCyc:G185E-7003-MONOMER
    MTBH37RV:G185E-7003-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P9WG57

    Family and domain databases

    Gene3Di3.30.70.3180, 2 hits
    HAMAPiMF_01408 ThyX, 1 hit
    InterProiView protein in InterPro
    IPR003669 Thymidylate_synthase_ThyX
    IPR036098 Thymidylate_synthase_ThyX_sf
    PANTHERiPTHR34934 PTHR34934, 1 hit
    PfamiView protein in Pfam
    PF02511 Thy1, 1 hit
    SUPFAMiSSF69796 SSF69796, 1 hit
    TIGRFAMsiTIGR02170 thyX, 1 hit
    PROSITEiView protein in PROSITE
    PS51331 THYX, 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 nameiTHYX_MYCTU
    <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: P9WG57
    Secondary accession number(s): L0TD90, O33296, P66930
    <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: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: November 13, 2019
    This is version 32 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 programProkaryotic 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. SIMILARITY comments
      Index of protein domains and families
    2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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