Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0AF12 (MTNN_ECOLI)

Entry version 128 (02 Dec 2020)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
Add a publicationFeedback
Protein

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Gene

mtnN

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

Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively (PubMed:3911944, PubMed:16101288). Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation (PubMed:15911379). Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates in vitro (PubMed:3911944).3 Publications

<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

Strongly inhibited by aryl-substituted MTA analogs, alkyl-substituted MTA analogs, 5'-methylthioformycin, 5'-chloroformycin, S-formycinylhomocysteine, 5'-methylthiotubercidin, S-tubercidinylhomocysteine and S-8-aza-adenosylhomocysteine. Poorly inhibited by 5'-isobutylthioinosine, 5'-n-butylthioinosine, 5'-methylthio-3-deaza-adenosine, 5'-isobutylthio-3-deaza-adenosine, S-n-6-methyl-3-deaza-adenosylhomocysteine, S-adenosylhomocysteine sulphoxide and Sinefungin.4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 3.0 sec(-1) and 2.6 sec(-1) with 5'-methylthioadenosine and S-adenosylhomocysteine as substrate, respectively.1 Publication
  1. KM=0.4 µM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius)1 Publication
  2. KM=0.8 µM for 5'-methylthioadenosine (at pH 7 and 22 degrees Celsius)1 Publication
  3. KM=4.3 µM for S-adenosylhomocysteine (at pH 7 and 37 degrees Celsius)1 Publication
  4. KM=1.3 µM for S-adenosylhomocysteine (at pH 7 and 22 degrees Celsius)1 Publication

    pH dependencei

    Exhibits activity across a broad pH range. Enzyme activity is moderately improved under acidic conditions.1 Publication

    Temperature dependencei

    Optimum temperature is 37-45 degrees Celsius. Rapidly inactivated after exposure for 10 minutes at 55 degrees Celsius.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: 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).UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN), 5'-methylthioadenosine/S-adenosylhomocysteine 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 <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei12Proton acceptorUniRule annotation1 Publication1
    <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 sitei78Substrate; via amide nitrogenUniRule annotation1 Publication1
    Binding sitei152Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication1
    Active sitei197Proton donorUniRule annotation1 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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, Methionine biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG11090-MONOMER
    MetaCyc:EG11090-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.2.2.30, 2026
    3.2.2.9, 2026

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

    More...    UniPathwayi    		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%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:
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase1 PublicationUniRule annotation (EC:3.2.2.9UniRule annotation3 Publications)
    Short name:
    MTA/SAH nucleosidaseUniRule annotation
    Short name:
    MTAN1 PublicationUniRule annotation
    Alternative name(s):
    5'-deoxyadenosine nucleosidaseUniRule annotation1 Publication
    Short name:
    DOA nucleosidaseUniRule annotation1 Publication
    Short name:
    dAdo nucleosidaseUniRule annotation1 Publication
    5'-methylthioadenosine nucleosidaseUniRule annotation
    Short name:
    MTA nucleosidaseUniRule annotation
    S-adenosylhomocysteine nucleosidaseUniRule annotation
    Short name:
    AdoHcy nucleosidaseUniRule annotation
    Short name:
    SAH nucleosidaseUniRule annotation
    Short name:
    SRH nucleosidaseUniRule 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:mtnNUniRule annotation
    Synonyms:mtn, pfs, yadA
    Ordered Locus Names:b0159, JW0155
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    <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

    Complete GO annotation on QuickGO ...

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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

    Cells lacking this gene are deficient in biotin synthase (BioB) activity in vivo due to accumulation of 5'-deoxyadenosine.1 Publication

    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>Mutagenesisi9M → A: 13-19% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi12E → A or Q: Loss of catalytic activity. 1 Publication1
    Mutagenesisi50I → A: 12-23% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi76S → A: 13-23% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi151F → A: 0.5% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi173M → A: 0.5% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi174E → A or Q: Loss of catalytic activity. 1 Publication1
    Mutagenesisi193R → A: 13-28% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi196S → A: 2-4% of wild-type catalytic efficiency. 1 Publication1
    Mutagenesisi197D → A or N: Loss of catalytic activity. 1 Publication1
    Mutagenesisi207F → A: 2% of wild-type catalytic efficiency. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL2866

    Drug and drug target database

    More...    DrugBanki    		DB02158, (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol
    DB08606, (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL
    DB02933, 5'-Deoxy-5'-(Methylthio)-Tubercidin
    DB00173, Adenine
    DB02281, Formycin

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001644391 – 2325'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseAdd BLAST232

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0AF12

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

    More...    PaxDbi    		P0AF12

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0AF12

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...    SWISS-2DPAGEi    		P0AF12

    <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.

    UniRule annotation4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    P0AF12
    With#Exp.IntAct
    itself2EBI-1114261,EBI-1114261

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260991, 38 interactors
    852836, 1 interactor

    Database of interacting proteins

    More...    DIPi    		DIP-10270N

    Protein interaction database and analysis system

    More...    IntActi    		P0AF12, 7 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0159

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P0AF12

    <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

    1232
    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    		P0AF12

    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    		P0AF12

    <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>Regioni173 – 174Substrate bindingUniRule annotation2

    <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 PNP/UDP phosphorylase family. MtnN subfamily.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0775, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_031248_2_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0AF12

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0AF12

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.1580, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01684, Salvage_MtnN, 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%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.

    P0AF12-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI 
            60         70         80         90        100
    GKVAAALGAT LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA 
           110        120        130        140        150
    DVTAFGYEYG QLPGCPAGFK ADDKLIAAAE ACIAELNLNA VRGLIVSGDA 
           160        170        180        190        200
    FINGSVGLAK IRHNFPQAIA VEMEATAIAH VCHNFNVPFV VVRAISDVAD 
           210        220        230 
    QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG
    Length:232
    Mass (Da):24,354
    Last modified:December 20, 2005 - 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:i9B1FF9BEC39D4F2C
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA23678 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti212 – 232AVAAK…KLAHG → LLPLNSPA in AAA23678 (PubMed:2157212).CuratedAdd BLAST21
    Sequence conflicti212 – 232AVAAK…KLAHG → LLPLNSPA in AAA24322 (PubMed:2157212).CuratedAdd BLAST21

    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
    		M31772 Genomic DNA Translation: AAA23678.1 Different initiation.
    U24438 Genomic DNA Translation: AAC38291.1
    M83735 Genomic DNA Translation: AAA24322.1
    U70214 Genomic DNA Translation: AAB08589.1
    U00096 Genomic DNA Translation: AAC73270.1
    AP009048 Genomic DNA Translation: BAB96736.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S45227

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414701.1, NC_000913.3
    WP_000689844.1, NZ_SSZK01000004.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73270; AAC73270; b0159
    BAB96736; BAB96736; BAB96736

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		49586023
    948542

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0155
    eco:b0159

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2121

    <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
    		M31772 Genomic DNA Translation: AAA23678.1 Different initiation.
    U24438 Genomic DNA Translation: AAC38291.1
    M83735 Genomic DNA Translation: AAA24322.1
    U70214 Genomic DNA Translation: AAB08589.1
    U00096 Genomic DNA Translation: AAC73270.1
    AP009048 Genomic DNA Translation: BAB96736.1
    PIRiS45227
    RefSeqiNP_414701.1, NC_000913.3
    WP_000689844.1, NZ_SSZK01000004.1

    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
    1JYSX-ray1.90A/B1-232[»]
    1NC1X-ray2.00A/B1-232[»]
    1NC3X-ray2.20A/B1-232[»]
    1Y6QX-ray2.20A/B1-232[»]
    1Y6RX-ray2.20A/B1-232[»]
    1Z5NX-ray2.10A/B1-232[»]
    1Z5OX-ray2.00A/B1-232[»]
    1Z5PX-ray2.00A1-232[»]
    3O4VX-ray1.75A/B1-232[»]
    4WKCX-ray1.64A1-232[»]
    4YMLX-ray1.75A1-232[»]
    SMRiP0AF12
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260991, 38 interactors
    852836, 1 interactor
    DIPiDIP-10270N
    IntActiP0AF12, 7 interactors
    STRINGi511145.b0159

    Chemistry databases

    BindingDBiP0AF12
    ChEMBLiCHEMBL2866
    DrugBankiDB02158, (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol
    DB08606, (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL
    DB02933, 5'-Deoxy-5'-(Methylthio)-Tubercidin
    DB00173, Adenine
    DB02281, Formycin

    2D gel databases

    SWISS-2DPAGEiP0AF12

    Proteomic databases

    jPOSTiP0AF12
    PaxDbiP0AF12
    PRIDEiP0AF12

    Genome annotation databases

    EnsemblBacteriaiAAC73270; AAC73270; b0159
    BAB96736; BAB96736; BAB96736
    GeneIDi49586023
    948542
    KEGGiecj:JW0155
    eco:b0159
    PATRICifig|1411691.4.peg.2121

    Organism-specific databases

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

    More...    EchoBASEi    		EB1082

    Phylogenomic databases

    eggNOGiCOG0775, Bacteria
    HOGENOMiCLU_031248_2_2_6
    InParanoidiP0AF12
    PhylomeDBiP0AF12

    Enzyme and pathway databases

    UniPathwayiUPA00904;UER00871
    BioCyciEcoCyc:EG11090-MONOMER
    MetaCyc:EG11090-MONOMER
    BRENDAi3.2.2.30, 2026
    3.2.2.9, 2026

    Miscellaneous databases

    EvolutionaryTraceiP0AF12

    Protein Ontology

    More...    PROi    		PR:P0AF12

    Family and domain databases

    Gene3Di3.40.50.1580, 1 hit
    HAMAPiMF_01684, Salvage_MtnN, 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...

    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 nameiMTNN_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: P0AF12
    Secondary accession number(s): P24247
    <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: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: December 2, 2020
    This is version 128 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again