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Entry version 88 (16 Oct 2019)
Sequence version 1 (01 Mar 2001)
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Protein

Nucleoside kinase

Gene

Ta0880

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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

Nucleoside kinase with broad substrate specificity. Catalyzes the phosphorylation of a variety of nucleosides to the corresponding nucleoside 5'-mono-phosphate in the presence of phosphate donors and divalent cations. Displays the most efficient activity with guanosine, followed by inosine, cytidine, and adenosine. Negligible enzymatic activity is detected with thymidine, uridine, and 2-deoxyadenosine. ATP is the most efficient phosphate donor, but can also use GTP and ITP. Shows no sugar kinase activity, since it is unable to phosphorylate ribose, fructose-1-phosphate, or fructose-6-phosphate.1 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

Mg2+1 Publication, Co2+1 PublicationNote: Can use Mg2+ and Co2+ with equal efficiency in vitro, and to a lesser extent, Mn2+, but not Ni2+.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 0.072 sec(-1) with ATP and guanosine as substrates. kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1) with ATP and adenosine as substrates. kcat is 0.27 sec(-1) with GTP and inosine as substrates (at pH 8.0 and 22 degrees Celsius).1 Publication
  1. KM=0.208 µM for guanosine (at pH 8.0 and 22 degrees Celsius)1 Publication
  2. KM=0.712 µM for inosine (at pH 8.0 and 22 degrees Celsius)1 Publication
  3. KM=0.411 µM for cytidine (at pH 8.0 and 22 degrees Celsius)1 Publication
  4. KM=1.12 µM for adenosine (at pH 8.0 and 22 degrees Celsius)1 Publication
  5. KM=46.9 µM for ATP (at pH 8.0 and 22 degrees Celsius)1 Publication
  6. KM=185 µM for GTP (at pH 8.0 and 22 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.6. Significant activity is observed over the pH range of 6.4 to 7.8. Enzymatic activity decreases markedly at pH 8.0 and at pH 6.2 and below.1 Publication

    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 sitei13SubstrateBy similarity1
    Binding sitei28SubstrateBy similarity1
    Binding sitei38Substrate; via amide nitrogenBy similarity1
    Binding sitei42SubstrateBy similarity1
    Binding sitei102ATPBy similarity1
    Binding sitei104SubstrateBy similarity1
    Binding sitei150SubstrateBy similarity1
    Binding sitei173ATPBy similarity1
    <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 sitei227Proton acceptorBy similarity1
    Binding sitei227SubstrateBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei230Transition state stabilizerBy similarity1

    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 bindingi196 – 201ATPBy similarity6

    <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
    LigandATP-binding, Cobalt, GTP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    TACI273075:G1GT7-977-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.1.B20 6324

    <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:
    Nucleoside kinase1 Publication
    Short name:
    NK1 Publication
    Alternative name(s):
    Adenosine kinase1 Publication (EC:2.7.1.201 Publication)
    Broad specificity nucleoside kinase1 Publication
    Cytidine kinase1 Publication (EC:2.7.1.2131 Publication)
    Guanosine kinase1 Publication (EC:2.7.1.-1 Publication)
    Inosine kinase1 Publication (EC:2.7.1.731 Publication)
    <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
    Ordered Locus Names:Ta0880Imported
    <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>OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
    <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 identifieri273075 [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 lineageiArchaeaEuryarchaeotaDiaforarchaea groupThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    <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
    • UP000001024 <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

    <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_00004399481 – 287Nucleoside kinaseAdd BLAST287

    <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.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    273075.Ta0880

    <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

    1287
    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
    Q9HJT3

    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
    Q9HJT3

    <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 carbohydrate kinase PfkB family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG00014 Archaea
    COG0524 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000142559

    KEGG Orthology (KO)

    More...
    KOi
    K22026

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    AAQVGCM

    Database of Orthologous Groups

    More...
    OrthoDBi
    98664at2157

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.20.150.10, 1 hit
    3.40.1190.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR023314 Myo_inos_iolC-like_sf
    IPR011611 PfkB_dom
    IPR029056 Ribokinase-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00294 PfkB, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53613 SSF53613, 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.

    Q9HJT3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRFLAYFGHL NIDVLISVDS IPREGSVNVK DLRPRFGGTA GNFAIVAQKF
    60 70 80 90 100
    RIPFDLYSAV GMKTHREYLA MIESMGINTG HVEKFEDESG PICYIATDGK
    110 120 130 140 150
    KQVSFMHQGA MEKWKPQLAD EYEYVHFSTG PNYLDMAKSI RSKIIFDPSQ
    160 170 180 190 200
    EIHKYSKDEL KKFHEISYMS IFNDHEYRVF REMTGLSSPK VTTIVTNGER
    210 220 230 240 250
    GSSLFMDGKK YDFPAIPSSG DTVGAGDSFR AGLYLALYNR RSIEKGMIYG
    260 270 280
    TIIAHHVIDD GIENFSLNME DLERETENYR RMFTKRS
    Length:287
    Mass (Da):32,805
    Last modified:March 1, 2001 - 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:i24CF1E8CE10466F8
    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
    AL445065 Genomic DNA Translation: CAC12009.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_010901290.1, NC_002578.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAC12009; CAC12009; CAC12009

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1456419

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tac:Ta0880

    <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
    AL445065 Genomic DNA Translation: CAC12009.1
    RefSeqiWP_010901290.1, NC_002578.1

    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
    3BF5X-ray1.91A/B1-287[»]
    SMRiQ9HJT3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi273075.Ta0880

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    1456419

    Genome annotation databases

    EnsemblBacteriaiCAC12009; CAC12009; CAC12009
    GeneIDi1456419
    KEGGitac:Ta0880

    Phylogenomic databases

    eggNOGiarCOG00014 Archaea
    COG0524 LUCA
    HOGENOMiHOG000142559
    KOiK22026
    OMAiAAQVGCM
    OrthoDBi98664at2157

    Enzyme and pathway databases

    BioCyciTACI273075:G1GT7-977-MONOMER
    BRENDAi2.7.1.B20 6324

    Miscellaneous databases

    EvolutionaryTraceiQ9HJT3

    Family and domain databases

    Gene3Di2.20.150.10, 1 hit
    3.40.1190.20, 1 hit
    InterProiView protein in InterPro
    IPR023314 Myo_inos_iolC-like_sf
    IPR011611 PfkB_dom
    IPR029056 Ribokinase-like
    PfamiView protein in Pfam
    PF00294 PfkB, 1 hit
    SUPFAMiSSF53613 SSF53613, 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 nameiNK_THEAC
    <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: Q9HJT3
    <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: May 10, 2017
    Last sequence update: March 1, 2001
    Last modified: October 16, 2019
    This is version 88 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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