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Entry version 110 (08 May 2019)
Sequence version 1 (01 May 1999)
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Protein

Aminodeoxyfutalosine nucleosidase

Gene

mtnN

Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
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 direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.2 Publications

<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 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 the transition state analog BuT-DADMe-ImmA. This compound is also able to inhibit H.pylori growth and is more efficient than antibiotics commonly used in ulcer therapy.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 12.1 sec(-1) with 5'-methylthioadenosine as substrate, and 4.3 sec(-1) with aminodeoxyfutalosine as substrate (PubMed:22891633). kcat is 4.92 sec(-1) with 5'-methylthioadenosine as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:20954236).2 Publications
  1. KM=0.6 µM for 5'-methylthioadenosine2 Publications
  2. KM=0.8 µM for aminodeoxyfutalosine2 Publications
  3. KM=44.9 µM for 5'-methylthioadenosine (at pH 7.5 and 37 degrees Celsius)2 Publications

    <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: menaquinone biosynthesis

    This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.
    View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

    Pathwayi: L-methionine biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Aminodeoxyfutalosine nucleosidase (mtnN)
    2. no protein annotated in this organism
    This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei13Proton acceptor1 Publication1
    <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 sitei80Substrate; via amide nitrogenBy similarity1
    Binding sitei154Substrate; via amide nitrogen and carbonyl oxygen1
    Active sitei198Proton donor1 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 processAmino-acid biosynthesis, Menaquinone biosynthesis, Methionine biosynthesis

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.2.30 2604
    3.2.2.9 2604

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

    More...
    UniPathwayi
    UPA00079

    UPA00904;UER00871

    <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:
    Aminodeoxyfutalosine nucleosidase (EC:3.2.2.302 Publications)
    Short name:
    AFL nucleosidase
    Short name:
    Aminofutalosine nucleosidase
    Alternative name(s):
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC:3.2.2.92 Publications)
    Short name:
    MTA/SAH nucleosidase
    Short name:
    MTAN
    6-amino-6-deoxyfutalosine N-ribosylhydrolase
    <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:mtnN
    Synonyms:mtn
    Ordered Locus Names:jhp_0082
    <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>OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
    <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 identifieri85963 [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 lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    <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
    • UP000000804 <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_00001644441 – 230Aminodeoxyfutalosine nucleosidaseAdd BLAST230

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

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

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    85963.jhp_0082

    <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

    1230
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    3NM4X-ray1.70A/B1-230[»]
    3NM5X-ray1.80A/B1-230[»]
    3NM6X-ray1.60B1-230[»]
    4FFSX-ray1.90A1-230[»]
    4OJTX-ray1.50A2-230[»]
    4OY3X-ray1.20A2-230[»]
    4P54X-ray1.65A2-230[»]
    4WKNX-ray2.00A2-230[»]
    4WKOX-ray1.90A2-230[»]
    4WKPX-ray1.58A/B/C/D2-230[»]
    4YNBX-ray2.00A2-230[»]
    4YO8X-ray2.10A/B2-230[»]
    5CCDOther2.20A2-230[»]
    5CCEOther2.50A2-230[»]
    5JPCOther2.50A2-230[»]
    5K1ZOther2.60A2-230[»]
    5KB3X-ray1.40A2-230[»]

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

    More...
    SMRi
    Q9ZMY2

    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
    Q9ZMY2

    <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>Regioni174 – 175Substrate binding2

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105DUF Bacteria
    COG0775 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K18284

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DQFVHSK

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1580, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR010049 MTA_SAH_Nsdase
    IPR000845 Nucleoside_phosphorylase_d
    IPR035994 Nucleoside_phosphorylase_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01048 PNP_UDP_1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53167 SSF53167, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01704 MTA/SAH-Nsdase, 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.

    Q9ZMY2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQKIGILGAM REEITPILEL FGVDFEEIPL GGNVFHKGVY HNKEIIVAYS
    60 70 80 90 100
    KIGKVHSTLT TTSMILAFGV QKVLFSGVAG SLVKDLKIND LLVATQLVQH
    110 120 130 140 150
    DVDLSAFDHP LGFIPESAIF IETSGSLNAL AKKIANEQHI ALKEGVIASG
    160 170 180 190 200
    DQFVHSKERK EFLVSEFKAS AVEMEGASVA FVCQKFGVPC CVLRSISDNA
    210 220 230
    DEKAGMSFDE FLEKSAHTSA KFLKSMVDEL
    Length:230
    Mass (Da):25,020
    Last modified:May 1, 1999 - 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:iF1E128A8160512C9
    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
    AE001439 Genomic DNA Translation: AAD05666.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E71976

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAD05666; AAD05666; jhp_0082

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hpj:jhp_0082

    <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
    AE001439 Genomic DNA Translation: AAD05666.1
    PIRiE71976

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NM4X-ray1.70A/B1-230[»]
    3NM5X-ray1.80A/B1-230[»]
    3NM6X-ray1.60B1-230[»]
    4FFSX-ray1.90A1-230[»]
    4OJTX-ray1.50A2-230[»]
    4OY3X-ray1.20A2-230[»]
    4P54X-ray1.65A2-230[»]
    4WKNX-ray2.00A2-230[»]
    4WKOX-ray1.90A2-230[»]
    4WKPX-ray1.58A/B/C/D2-230[»]
    4YNBX-ray2.00A2-230[»]
    4YO8X-ray2.10A/B2-230[»]
    5CCDOther2.20A2-230[»]
    5CCEOther2.50A2-230[»]
    5JPCOther2.50A2-230[»]
    5K1ZOther2.60A2-230[»]
    5KB3X-ray1.40A2-230[»]
    SMRiQ9ZMY2
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi85963.jhp_0082

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD05666; AAD05666; jhp_0082
    KEGGihpj:jhp_0082

    Phylogenomic databases

    eggNOGiENOG4105DUF Bacteria
    COG0775 LUCA
    KOiK18284
    OMAiDQFVHSK

    Enzyme and pathway databases

    UniPathwayi
    UPA00079

    UPA00904;UER00871

    BRENDAi3.2.2.30 2604
    3.2.2.9 2604

    Miscellaneous databases

    EvolutionaryTraceiQ9ZMY2

    Protein Ontology

    More...
    PROi
    PR:Q9ZMY2

    Family and domain databases

    Gene3Di3.40.50.1580, 1 hit
    InterProiView protein in InterPro
    IPR010049 MTA_SAH_Nsdase
    IPR000845 Nucleoside_phosphorylase_d
    IPR035994 Nucleoside_phosphorylase_sf
    PfamiView protein in Pfam
    PF01048 PNP_UDP_1, 1 hit
    SUPFAMiSSF53167 SSF53167, 1 hit
    TIGRFAMsiTIGR01704 MTA/SAH-Nsdase, 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 nameiMQMTN_HELPJ
    <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: Q9ZMY2
    <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 30, 2000
    Last sequence update: May 1, 1999
    Last modified: May 8, 2019
    This is version 110 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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