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Entry version 59 (26 Feb 2020)
Sequence version 1 (03 Apr 2007)
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Protein

Thiamine-monophosphate kinase

Gene

thiL

Organism
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
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 ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.UniRule annotation1 Publication

Miscellaneous

Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">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 inhibited by AMP; the mode of AMP inhibition is uncompetitive for both TMP and ATP.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

kcat is 0.063 sec(-1) (at pH 7.0 and 100 degrees Celsius).1 Publication
  1. KM=0.20 µM for thiamine phosphate (at pH 7.0 and 100 degrees Celsius)1 Publication
  2. KM=39 µM for ATP (at pH 7.0 and 100 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is around 7.0. Retains about 90% of maximum activity at pH 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 120 degrees Celsius. Activities at 100 and 80 degrees Celsius are about 50% and 10% of that at 120 degrees Celsius, respectively. Is unstable so that the protein loses about 45% of its activity after heating for 15 minutes at 100 degrees Celsius. However, the enzyme is not so intensively inactivated in the presence of ATP.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: thiamine diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes thiamine diphosphate from thiamine phosphate.UniRule annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Thiamine-monophosphate kinase (thiL)
    This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine diphosphate from thiamine phosphate, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi25Magnesium 3UniRule annotation1
    Metal bindingi25Magnesium 4; via carbonyl oxygenUniRule annotation1
    Metal bindingi39Magnesium 1; via carbonyl oxygenUniRule annotation1
    Metal bindingi40Magnesium 1UniRule annotation1
    Metal bindingi40Magnesium 2UniRule annotation1
    Metal bindingi68Magnesium 2UniRule annotation1
    Metal bindingi68Magnesium 3UniRule annotation1
    Metal bindingi68Magnesium 4UniRule annotation1
    Metal bindingi113Magnesium 1UniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei136ATPUniRule annotation1
    Metal bindingi194Magnesium 3UniRule annotation1
    Binding sitei196ATPUniRule annotation1
    Metal bindingi197Magnesium 5UniRule annotation1
    Binding sitei243SubstrateUniRule annotation1
    Binding sitei286SubstrateUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi112 – 113ATPUniRule annotation2

    <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 functionKinase, Transferase
    Biological processThiamine biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    PCAL410359:GIX2-649-MONOMER

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

    More...
    UniPathwayi
    UPA00060;UER00142

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Thiamine-monophosphate kinaseUniRule annotation (EC:2.7.4.16UniRule annotation1 Publication)
    Short name:
    TMP kinaseUniRule annotation
    Short name:
    TP kinase1 Publication
    Short name:
    Thiamine-phosphate kinase1 PublicationUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:thiL1 Publication
    Ordered Locus Names:Pcal_0657Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiPyrobaculum calidifontis (strain JCM 11548 / VA1)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri410359 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000001431 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi136R → M: 7-fold decrease in affinity for ATP. 1.5-fold increase in activity. 1 Publication1
    Mutagenesisi196S → A: 90% decrease in activity. However, displays a 30-fold increase in the catalytic efficiency toward ATP due to a large increase in affinity for ATP. 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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004398881 – 293Thiamine-monophosphate kinaseAdd BLAST293

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    410359.Pcal_0657

    <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

    <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 thiamine-monophosphate kinase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG00638 Archaea
    COG0611 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_046964_2_1_2

    KEGG Orthology (KO)

    More...
    KOi
    K00946

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DFGWRNV

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02194 ThiL, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1330.10, 1 hit
    3.90.650.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02128 TMP_kinase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf
    IPR006283 ThiL

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR30270 PTHR30270, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00586 AIRS, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55326 SSF55326, 1 hit
    SSF56042 SSF56042, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    A3MTW6-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSGFGGRGVD EKGFLRWLLG ELGVEEDDVA YVDGLVVKVD GAAASTSRLP
    60 70 80 90 100
    FQTWADFGWR NVAAAYSDVR VKFAEARLLL ASVTAPDLGT AAEVVQGVRE
    110 120 130 140 150
    ASQFFSLAYV GGDLNEGRDV VVDVVLVGWA RARVGRAPRP GDVLVTIPQF
    160 170 180 190 200
    GYTSLAYRFW QMGGAVVERG VEALKRPKPL WPLPPAECVT AAMDSSDGLG
    210 220 230 240 250
    DVLWSMARGV DIVVKELPAP REVLEFAAER GLDVGEIVFN GGEEFLPVFA
    260 270 280 290
    VRRDCPVESP YVSFAEVVPG EGRVWWRGEE LKWRGWAYFR GWG
    Length:293
    Mass (Da):32,000
    Last modified:April 3, 2007 - 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:i62778CDB7900822F
    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
    CP000561 Genomic DNA Translation: ABO08083.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABO08083; ABO08083; Pcal_0657

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    pcl:Pcal_0657

    <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
    CP000561 Genomic DNA Translation: ABO08083.1

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein-protein interaction databases

    STRINGi410359.Pcal_0657

    Genome annotation databases

    EnsemblBacteriaiABO08083; ABO08083; Pcal_0657
    KEGGipcl:Pcal_0657

    Phylogenomic databases

    eggNOGiarCOG00638 Archaea
    COG0611 LUCA
    HOGENOMiCLU_046964_2_1_2
    KOiK00946
    OMAiDFGWRNV

    Enzyme and pathway databases

    UniPathwayiUPA00060;UER00142
    BioCyciPCAL410359:GIX2-649-MONOMER

    Family and domain databases

    CDDicd02194 ThiL, 1 hit
    Gene3Di3.30.1330.10, 1 hit
    3.90.650.10, 1 hit
    HAMAPiMF_02128 TMP_kinase, 1 hit
    InterProiView protein in InterPro
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf
    IPR006283 ThiL
    PANTHERiPTHR30270 PTHR30270, 1 hit
    PfamiView protein in Pfam
    PF00586 AIRS, 1 hit
    SUPFAMiSSF55326 SSF55326, 1 hit
    SSF56042 SSF56042, 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 nameiTHIL_PYRCJ
    <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: A3MTW6
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
    Last sequence update: April 3, 2007
    Last modified: February 26, 2020
    This is version 59 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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