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UniProtKB - P0AF18 (NAGA_ECOLI)

Entry version 118 (07 Apr 2021)
Sequence version 1 (20 Dec 2005)
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Protein

N-acetylglucosamine-6-phosphate deacetylase

Gene

nagA

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

Involved in the first step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. In vitro, can also hydrolyze substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate, N-trifluoroacetyl-D-glucosamine-6-phosphate, N-acetyl-D-glucosamine-6-sulfate, N-acetyl-D-galactosamine-6-phosphate, and N-formyl-D-glucosamine-6-phosphate.6 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 '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

Zn2+3 Publications, Co2+3 Publications, Mn2+3 Publications, Cd2+3 Publications, Fe2+3 Publications, Ni2+3 PublicationsNote: Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn2+ and Co2+, followed by Mn2+, Cd2+, Fe2+ and Ni2+.3 Publications

<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

Inhibited by high substrate concentration and by products glucosamine 6-phosphate and acetate. Completely inactivated by the treatment with 5,5'-dithio-bis(2-nitrobenzoate) or 2,2'-dithio-pyridine (2-DPDS). Inhibited by 1,10-phenanthroline and EDTA.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 102 sec(-1) for the deacetylation of N-acetyl-D-glucosamine-6-phosphate by the Zn-enzyme. The Cd-NagA catalyzes the hydrolysis of N-thioacetyl-D-glucosamine-6-phosphate substrate about an order of magnitude better than does the Zn-substituted enzyme. The N-trifluoroacetyl substituted substrate is hydrolyzed 26 times faster than the natural substrate, but the N-formyl substrate is hydrolyzed more slowly by a factor of 5.3 Publications
  1. KM=0.3 mM for N-acetyl-glucosamine 6-phosphate (at 30 degrees Celsius and pH 7.5)3 Publications
  2. KM=0.8 mM for N-acetyl-glucosamine 6-phosphate (at 37 degrees Celsius and pH 8.0)3 Publications
  3. KM=20 mM for glucosamine 6-phosphate (at 30 degrees Celsius and pH 7.5)3 Publications
  4. KM=20 mM for acetate (at 30 degrees Celsius and pH 7.5)3 Publications
  5. KM=0.08 mM for N-acetyl-D-glucosamine-6-phosphate (at 30 degrees Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)3 Publications
  6. KM=1.24 mM for N-acetyl-D-galactosamine-6-phosphate (at 30 degrees Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)3 Publications

    pH dependencei

    Optimum pH is 8.5.3 Publications

    <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: N-acetylneuraminate degradation

    This protein is involved in step 4 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.1 Publication
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA)
    2. N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK)
    3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE), Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
    4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
    5. Glucosamine-6-phosphate deaminase (nagB), Glucosamine-6-phosphate deaminase (nagB)
    This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi131Zinc1 Publication1
    Metal bindingi195Zinc; via tele nitrogen1 Publication1
    Metal bindingi216Zinc; via tele nitrogen1 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 sitei227Substrate1 Publication1
    <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 sitei273Proton donor/acceptor1 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 processCarbohydrate metabolism
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:NAG6PDEACET-MONOMER
    MetaCyc:NAG6PDEACET-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.5.1.25, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P0AF18

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

    More...    UniPathwayi    		UPA00629;UER00683

    <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:
    N-acetylglucosamine-6-phosphate deacetylase1 Publication (EC:3.5.1.255 Publications)
    Short name:
    GlcNAc 6-P deacetylase1 Publication
    <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:nagA
    Ordered Locus Names:b0677, JW0663
    <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 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

    Synthesizes high levels of glucosamine-6-phosphate deaminase and over half of the amount of glucosamine-6-phosphate synthase compared to wild-type.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>Mutagenesisi59Q → H: Large decrease in catalytic activity and substrate affinity, and increase in the average amount of Zn bound to the protein, suggesting that an additional metal ion can bind to this mutant; when associated with H-61. 2 Publications1
    Mutagenesisi61N → H: Large decrease in catalytic activity and substrate affinity, and increase in the average amount of Zn bound to the protein, suggesting that an additional metal ion can bind to this mutant; when associated with H-59. 1 Publication1
    Mutagenesisi131E → Q or A: Large reduction in the amount of the metal cofactor bound to the enzyme. 1 Publication1
    Mutagenesisi143H → N: Dramatic decrease in catalytic activity and moderate decrease in substrate affinity, producing a 6000-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi143H → Q: 180-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi251H → N: 500-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi273D → N or A: Loss of catalytic 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001709151 – 382N-acetylglucosamine-6-phosphate deacetylaseAdd BLAST382

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0AF18

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

    More...    PaxDbi    		P0AF18

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0AF18

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By N-acetylglucosamine. Induced by low extracellular levels of magnesium via the PhoQ/PhoP two-component regulatory system.1 Publication

    <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

    Homotetramer.

    4 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4261208, 26 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-10297N

    Protein interaction database and analysis system

    More...    IntActi    		P0AF18, 5 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0677

    <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

    1382
    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    		P0AF18

    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    		P0AF18

    <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>Regioni142 – 143Substrate binding1 Publication2
    Regioni219 – 220Substrate binding1 Publication2
    Regioni248 – 251Substrate binding1 Publication4
    Regioni306 – 308Substrate binding1 Publication3

    <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 metallo-dependent hydrolases superfamily. NagA family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1820, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_032482_2_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0AF18

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0AF18

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00854, NagA, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		2.30.40.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR006680, Amidohydro-rel
    IPR003764, GlcNAc_6-P_deAcase
    IPR011059, Metal-dep_hydrolase_composite
    IPR032466, Metal_Hydrolase

    The PANTHER Classification System

    More...    PANTHERi    		PTHR11113:SF14, PTHR11113:SF14, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01979, Amidohydro_1, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF038994, NagA, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51338, SSF51338, 1 hit
    SSF51556, SSF51556, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00221, nagA, 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.

    P0AF18-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYALTQGRIF TGHEFLDDHA VVIADGLIKS VCPVAELPPE IEQRSLNGAI 
            60         70         80         90        100
    LSPGFIDVQL NGCGGVQFND TAEAVSVETL EIMQKANEKS GCTNYLPTLI 
           110        120        130        140        150
    TTSDELMKQG VRVMREYLAK HPNQALGLHL EGPWLNLVKK GTHNPNFVRK 
           160        170        180        190        200
    PDAALVDFLC ENADVITKVT LAPEMVPAEV ISKLANAGIV VSAGHSNATL 
           210        220        230        240        250
    KEAKAGFRAG ITFATHLYNA MPYITGREPG LAGAILDEAD IYCGIIADGL 
           260        270        280        290        300
    HVDYANIRNA KRLKGDKLCL VTDATAPAGA NIEQFIFAGK TIYYRNGLCV 
           310        320        330        340        350
    DENGTLSGSS LTMIEGVRNL VEHCGIALDE VLRMATLYPA RAIGVEKRLG 
           360        370        380 
    TLAAGKVANL TAFTPDFKIT KTIVNGNEVV TQ
    Length:382
    Mass (Da):40,949
    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:iA10B015ADFC98FCA
    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
    		X14135 Genomic DNA Translation: CAA32353.1
    AF052007 Genomic DNA Translation: AAC09325.1
    U00096 Genomic DNA Translation: AAC73771.1
    AP009048 Genomic DNA Translation: BAA35320.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A37018

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415203.1, NC_000913.3
    WP_000271153.1, NZ_STEB01000044.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73771; AAC73771; b0677
    BAA35320; BAA35320; BAA35320

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		57728780
    945289

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0663
    eco:b0677

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1601

    <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
    		X14135 Genomic DNA Translation: CAA32353.1
    AF052007 Genomic DNA Translation: AAC09325.1
    U00096 Genomic DNA Translation: AAC73771.1
    AP009048 Genomic DNA Translation: BAA35320.1
    PIRiA37018
    RefSeqiNP_415203.1, NC_000913.3
    WP_000271153.1, NZ_STEB01000044.1

    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
    1YMYX-ray2.60A/B1-382[»]
    1YRRX-ray2.00A/B1-382[»]
    2P50X-ray2.20A/B/C/D1-382[»]
    2P53X-ray2.10A/B1-382[»]
    SMRiP0AF18
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4261208, 26 interactors
    DIPiDIP-10297N
    IntActiP0AF18, 5 interactors
    STRINGi511145.b0677

    Proteomic databases

    jPOSTiP0AF18
    PaxDbiP0AF18
    PRIDEiP0AF18

    Genome annotation databases

    EnsemblBacteriaiAAC73771; AAC73771; b0677
    BAA35320; BAA35320; BAA35320
    GeneIDi57728780
    945289
    KEGGiecj:JW0663
    eco:b0677
    PATRICifig|1411691.4.peg.1601

    Organism-specific databases

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

    More...    EchoBASEi    		EB0626

    Phylogenomic databases

    eggNOGiCOG1820, Bacteria
    HOGENOMiCLU_032482_2_2_6
    InParanoidiP0AF18
    PhylomeDBiP0AF18

    Enzyme and pathway databases

    UniPathwayiUPA00629;UER00683
    BioCyciEcoCyc:NAG6PDEACET-MONOMER
    MetaCyc:NAG6PDEACET-MONOMER
    BRENDAi3.5.1.25, 2026
    SABIO-RKiP0AF18

    Miscellaneous databases

    EvolutionaryTraceiP0AF18

    Protein Ontology

    More...    PROi    		PR:P0AF18

    Family and domain databases

    CDDicd00854, NagA, 1 hit
    Gene3Di2.30.40.10, 1 hit
    InterProiView protein in InterPro
    IPR006680, Amidohydro-rel
    IPR003764, GlcNAc_6-P_deAcase
    IPR011059, Metal-dep_hydrolase_composite
    IPR032466, Metal_Hydrolase
    PANTHERiPTHR11113:SF14, PTHR11113:SF14, 1 hit
    PfamiView protein in Pfam
    PF01979, Amidohydro_1, 1 hit
    PIRSFiPIRSF038994, NagA, 1 hit
    SUPFAMiSSF51338, SSF51338, 1 hit
    SSF51556, SSF51556, 1 hit
    TIGRFAMsiTIGR00221, nagA, 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 nameiNAGA_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: P0AF18
    Secondary accession number(s): P15300
    <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: April 7, 2021
    This is version 118 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
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