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Protein

dITP/XTP pyrophosphatase

Gene

rdgB

Organism
Escherichia coli (strain K12)
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

Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP (PubMed:12297000, PubMed:17976651). Can also efficiently hydrolyze 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) (PubMed:17090528). Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions (PubMed:12297000, PubMed:12730170, PubMed:17090528). To a much lesser extent, is also able to hydrolyze GTP, dGTP and dUTP, but shows very low activity toward the canonical nucleotides dATP, dCTP and dTTP and toward 8-oxo-dGTP, purine deoxyribose triphosphate, 2-aminopurine deoxyribose triphosphate and 2,6-diaminopurine deoxyribose triphosphate (PubMed:12297000, PubMed:17090528).UniRule annotation4 Publications

Miscellaneous

Modified or damaged nucleotides such as 6-chloropurine deoxyribose triphosphate, 8-Br-dGTP, 5-Br-dCTP, 5-Br-dUTP, 7-deaza-dGTP, 7-methyl-GTP, N6-etheno-ATP, NAD, NADH, FAD, ADP-ribose, UPD-glucose, AppA and ApppA are not hydrolyzed by the enzyme.1 Publication
The aberrant nucleotides XTP and dITP can be produced by oxidative deamination from purine nucleotides in cells; they are potentially mutagenic.Curated

<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+2 Publications, Mn2+1 Publication, Ni2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Maximum activity is obtained with Mg2+. Activity with Mn2+ or Ni2+ makes up 60-75% of the maximum rate.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

Vmax values are similar for XTP, dITP and ITP. Activity toward dATP, dCTP and dTTP is less than 1% of the rate of XTP hydrolysis. dGTP and dUTP are hydrolyzed at 10-12% of the rate of XTP hydrolysis (PubMed:12297000). kcat is 5.7 sec(-1) with ITP or dHAPTP as substrate. kcat is 1.5 sec(-1) with dGTP as substrate (at pH 9.5 and 37 degrees Celsius) (PubMed:17090528). kcat is 19.9 sec(-1) with XTP as substrate. kcat is 13.2 sec(-1) with dITP as substrate. kcat is 18.9 sec(-1) with ITP as substrate. kcat is 0.85 sec(-1) with GTP as substrate. kcat is 0.37 sec(-1) with dGTP as substrate. kcat is 0.26 sec(-1) with TTP as substrate (at pH 9.0 and 37 degrees Celsius) (PubMed:17976651).3 Publications
  1. KM=0.33 mM for XTP (at pH 10.0 and 37 degrees Celsius)1 Publication
  2. KM=0.36 mM for dITP (at pH 10.0 and 37 degrees Celsius)1 Publication
  3. KM=0.41 mM for ITP (at pH 10.0 and 37 degrees Celsius)1 Publication
  4. KM=22.0 µM for dITP (at pH 9.5 and 37 degrees Celsius)1 Publication
  5. KM=792 µM for dGTP (at pH 9.5 and 37 degrees Celsius)1 Publication
  6. KM=16.5 µM for dHAPTP (at pH 9.5 and 37 degrees Celsius)1 Publication
  7. KM=23.3 µM for XTP (at pH 9.0 and 37 degrees Celsius)1 Publication
  8. KM=11.3 µM for dITP (at pH 9.0 and 37 degrees Celsius)1 Publication
  9. KM=5.6 µM for ITP (at pH 9.0 and 37 degrees Celsius)1 Publication
  10. KM=312.6 µM for GTP (at pH 9.0 and 37 degrees Celsius)1 Publication
  11. KM=181.5 µM for dGTP (at pH 9.0 and 37 degrees Celsius)1 Publication
  12. KM=289.1 µM for TTP (at pH 9.0 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 10-10.5 (PubMed:12297000). Optimum pH is 9.0 (PubMed:17976651). Reaction rates under neutral conditions are <40% of the maximum (PubMed:12297000).2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi40MagnesiumUniRule annotation1
    <p>This subsection of the ‘Function’ 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 sitei69Proton acceptor1 Publication1
    Metal bindingi69MagnesiumUniRule annotation1
    <p>This subsection of the ‘Function’ 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 sitei70Substrate; via amide nitrogenCombined sources1 Publication1
    Binding sitei177SubstrateCombined sources1 Publication1

    <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 functionHydrolase
    Biological processNucleotide metabolism
    LigandMagnesium, Manganese, Metal-binding, Nickel, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7530-MONOMER
    MetaCyc:G7530-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.6.1.19 2026

    <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:
    dITP/XTP pyrophosphataseUniRule annotation2 Publications (EC:3.6.1.66UniRule annotation2 Publications)
    Alternative name(s):
    Deoxyribonucleoside triphosphate pyrophosphohydrolase1 Publication
    Inosine triphosphate pyrophosphatase1 Publication
    Short name:
    ITPase1 Publication
    Non-canonical purine NTP pyrophosphataseUniRule annotation1 Publication
    Non-standard purine NTP pyrophosphataseUniRule annotation1 Publication
    Nucleoside-triphosphate diphosphataseUniRule annotation1 Publication
    Nucleoside-triphosphate pyrophosphataseUniRule annotation1 Publication
    Short name:
    NTPase1 PublicationUniRule 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:rdgBImported
    Synonyms:yggV
    Ordered Locus Names:b2954, JW2921
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG12982 rdgB

    <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

    GO - Cellular componenti

    <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

    Inactivation of this gene in a moa background (cells deficient in molybdopterin biosynthesis) results in increased N-6-hydroxylaminopurine (HAP) sensitivity, an increase in the level of mutagenesis, and increased recombination and SOS induction upon HAP exposure.1 Publication

    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>Mutagenesisi8T → A: Greatly reduced ITP pyrophosphatase activity. 1 Publication1
    Mutagenesisi10N → A: Greatly reduced ITP pyrophosphatase activity. 1 Publication1
    Mutagenesisi13K → A: Complete loss of enzymatic activity. 1 Publication1
    Mutagenesisi41E → A: Complete loss of enzymatic activity. 1 Publication1
    Mutagenesisi53K → A: Complete loss of enzymatic activity. 1 Publication1
    Mutagenesisi68D → A: Greatly reduced ITP pyrophosphatase activity. 1 Publication1
    Mutagenesisi69D → A: Complete loss of enzymatic activity. 1 Publication1
    Mutagenesisi71G → A: Greatly reduced ITP pyrophosphatase activity. 1 Publication1
    Mutagenesisi154F → A: Greatly reduced ITP pyrophosphatase activity. 1 Publication1
    Mutagenesisi160F → A: Greatly reduced ITP pyrophosphatase activity. 1 Publication1
    Mutagenesisi183R → A: Greatly reduced ITP pyrophosphatase activity. 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_00001781641 – 197dITP/XTP pyrophosphataseAdd BLAST197

    Proteomic databases

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

    More...
    PaxDbi
    P52061

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P52061

    <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.UniRule annotation2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260898, 103 interactors
    851750, 2 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P52061, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_3129

    <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

    1197
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P52061

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

    More...
    SMRi
    P52061

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P52061

    <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>Regioni8 – 13Substrate bindingUniRule annotationCombined sources1 Publication6
    Regioni154 – 157Substrate bindingUniRule annotationCombined sources1 Publication4
    Regioni182 – 183Substrate bindingUniRule annotationCombined sources1 Publication2

    <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 HAM1 NTPase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108V82 Bacteria
    COG0127 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000293319

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P52061

    KEGG Orthology (KO)

    More...
    KOi
    K02428

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P52061

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00515 HAM1, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.90.950.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01405 Non_canon_purine_NTPase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR020922 dITP/XTP_pyrophosphatase
    IPR002637 Ham1p-like
    IPR029001 ITPase-like_fam

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11067 PTHR11067, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01725 Ham1p_like, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52972 SSF52972, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00042 TIGR00042, 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>.<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.

    P52061-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQKVVLATGN VGKVRELASL LSDFGLDIVA QTDLGVDSAE ETGLTFIENA
    60 70 80 90 100
    ILKARHAAKV TALPAIADDS GLAVDVLGGA PGIYSARYSG EDATDQKNLQ
    110 120 130 140 150
    KLLETMKDVP DDQRQARFHC VLVYLRHAED PTPLVCHGSW PGVITREPAG
    160 170 180 190
    TGGFGYDPIF FVPSEGKTAA ELTREEKSAI SHRGQALKLL LDALRNG
    Length:197
    Mass (Da):21,039
    Last modified:October 1, 1996 - 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:i74E82A59B1A9E294
    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
    U28377 Genomic DNA Translation: AAA69121.1
    U00096 Genomic DNA Translation: AAC75991.1
    AP009048 Genomic DNA Translation: BAE77017.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A65081

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417429.1, NC_000913.3
    WP_001174777.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75991; AAC75991; b2954
    BAE77017; BAE77017; BAE77017

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947429

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2921
    eco:b2954

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3778

    <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
    U28377 Genomic DNA Translation: AAA69121.1
    U00096 Genomic DNA Translation: AAC75991.1
    AP009048 Genomic DNA Translation: BAE77017.1
    PIRiA65081
    RefSeqiNP_417429.1, NC_000913.3
    WP_001174777.1, NZ_LN832404.1

    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
    1K7KX-ray1.50A1-197[»]
    2PYUX-ray2.02A1-197[»]
    2Q16X-ray1.95A/B1-197[»]
    ProteinModelPortaliP52061
    SMRiP52061
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260898, 103 interactors
    851750, 2 interactors
    IntActiP52061, 3 interactors
    STRINGi316385.ECDH10B_3129

    Proteomic databases

    PaxDbiP52061
    PRIDEiP52061

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75991; AAC75991; b2954
    BAE77017; BAE77017; BAE77017
    GeneIDi947429
    KEGGiecj:JW2921
    eco:b2954
    PATRICifig|1411691.4.peg.3778

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB2807
    EcoGeneiEG12982 rdgB

    Phylogenomic databases

    eggNOGiENOG4108V82 Bacteria
    COG0127 LUCA
    HOGENOMiHOG000293319
    InParanoidiP52061
    KOiK02428
    PhylomeDBiP52061

    Enzyme and pathway databases

    BioCyciEcoCyc:G7530-MONOMER
    MetaCyc:G7530-MONOMER
    BRENDAi3.6.1.19 2026

    Miscellaneous databases

    EvolutionaryTraceiP52061

    Protein Ontology

    More...
    PROi
    PR:P52061

    Family and domain databases

    CDDicd00515 HAM1, 1 hit
    Gene3Di3.90.950.10, 1 hit
    HAMAPiMF_01405 Non_canon_purine_NTPase, 1 hit
    InterProiView protein in InterPro
    IPR020922 dITP/XTP_pyrophosphatase
    IPR002637 Ham1p-like
    IPR029001 ITPase-like_fam
    PANTHERiPTHR11067 PTHR11067, 1 hit
    PfamiView protein in Pfam
    PF01725 Ham1p_like, 1 hit
    SUPFAMiSSF52972 SSF52972, 1 hit
    TIGRFAMsiTIGR00042 TIGR00042, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiIXTPA_ECOLI
    <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: P52061
    Secondary accession number(s): Q2M9N9
    <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: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: December 5, 2018
    This is version 138 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
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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