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UniProtKB - P22106 (ASNB_ECOLI)

Protein

Asparagine synthetase B [glutamine-hydrolyzing]

Gene

asnB

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 ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity.3 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

Glutamine-dependent asparagine synthesis activity can be inhibited by aspartic acid analogs (such as a sulfinate derivative and (2S,3R)-2-amino-3-methylsuccinate) in vitro; the inhibition is competitive with respect to aspartate.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

  1. KM=17 mM for ammonia2 Publications
  2. KM=0.53 mM for aspartate (when assaying the ammonia-dependent synthetase reaction)2 Publications
  3. KM=0.85 mM for aspartate (when assaying the glutamine-dependent synthetase reaction)2 Publications
  4. KM=0.26 mM for ATP (when assaying the glutamine-dependent synthetase reaction)2 Publications
  5. KM=0.66 mM for glutamine (when assaying the glutamine-dependent synthetase reaction)2 Publications

    pH dependencei

    Optimum pH is 6.5-8.1 Publication

    <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: L-asparagine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
    Proteins known to be involved in this subpathway in this organism are:
    1. Asparagine synthetase B [glutamine-hydrolyzing] (asnB)
    This subpathway is part of the pathway L-asparagine biosynthesis, 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 L-asparagine from L-aspartate (L-Gln route), the pathway L-asparagine biosynthesis 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 sitei2For GATase activity1
    <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 sitei99Glutamine1
    Binding sitei233ATP; via carbonyl oxygen1
    Binding sitei273ATP; via amide nitrogen and carbonyl oxygen1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei349Important for beta-aspartyl-AMP intermediate formation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi347 – 348ATP2

    <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

    • amino acid binding Source: UniProtKB
    • asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB
    • aspartate-ammonia ligase activity Source: UniProtKB
    • ATP binding Source: UniProtKB
    • identical protein binding Source: IntAct
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the 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 functionLigase
    Biological processAmino-acid biosynthesis, Asparagine biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

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

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		6.3.5.4 2026

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

    More...    UniPathwayi
    UPA00134;UER00195

    Protein family/group databases

    MEROPS protease database

    More...    MEROPSi    		C44.976

    <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:
    Asparagine synthetase B [glutamine-hydrolyzing] (EC:6.3.5.4)
    Short name:
    AS-B
    <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:asnB
    Ordered Locus Names:b0674, JW0660
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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    		EG10092 asnB

    <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

    View the 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

    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>Mutagenesisi2C → A or S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity. 1 Publication1
    Mutagenesisi30H → A: 4,5-fold decrease in glutamine affinity. 1 Publication1
    Mutagenesisi34D → N or E: Little effect on the kinetic properties. 1 Publication1
    Mutagenesisi81H → A: 5-fold decrease in glutamine affinity. 1 Publication1
    Mutagenesisi105A → H: Little effect on the kinetic properties. 1 Publication1
    Mutagenesisi349E → A or Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity. 1 Publication1
    Mutagenesisi349E → D: 5-fold increase in affinity for asparate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00000569312 – 554Asparagine synthetase B [glutamine-hydrolyzing]Add BLAST553

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P22106

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

    More...    PaxDbi    		P22106

    PRoteomics IDEntifications database

    More...    PRIDEi    		P22106

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

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

    Homodimer.1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-549123,EBI-549123

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4261812, 416 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-9177N

    Protein interaction database and analysis system

    More...    IntActi    		P22106, 7 interactors

    STRING: functional protein association networks

    More...    STRINGi    		316385.ECDH10B_0739

    <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

    1554
    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    		P22106

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

    More...    SMRi    		P22106

    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    		P22106

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 186Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST185

    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>Regioni50 – 54Glutamine binding5
    Regioni75 – 77Glutamine binding3

    <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 asparagine synthetase family.Curated

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105CAQ Bacteria
    COG0367 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000027493

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P22106

    KEGG Orthology (KO)

    More...    KOi    		K01953

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P22106

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd01991 Asn_Synthase_B_C, 1 hit
    cd00712 AsnB, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.620, 1 hit
    3.60.20.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR006426 Asn_synth_AEB
    IPR001962 Asn_synthase
    IPR033738 AsnB_N
    IPR017932 GATase_2_dom
    IPR029055 Ntn_hydrolases_N
    IPR014729 Rossmann-like_a/b/a_fold

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00733 Asn_synthase, 1 hit
    PF13537 GATase_7, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001589 Asn_synthetase_glu-h, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF56235 SSF56235, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01536 asn_synth_AEB, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS51278 GATASE_TYPE_2, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P22106-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER 
            60         70         80         90        100
    LSIVDVNAGA QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC 
           110        120        130        140        150
    EVILALYQEK GPEFLDDLQG MFAFALYDSE KDAYLIGRDH LGIIPLYMGY 
           160        170        180        190        200
    DEHGQLYVAS EMKALVPVCR TIKEFPAGSY LWSQDGEIRS YYHRDWFDYD 
           210        220        230        240        250
    AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS SIISAITKKY 
           260        270        280        290        300
    AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF 
           310        320        330        340        350
    TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG 
           360        370        380        390        400
    SDEVFGGYLY FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA 
           410        420        430        440        450
    RVPFLDKKFL DVAMRINPQD KMCGNGKMEK HILRECFEAY LPASVAWRQK 
           460        470        480        490        500
    EQFSDGVGYS WIDTLKEVAA QQVSDQQLET ARFRFPYNTP TSKEAYLYRE 
           510        520        530        540        550
    IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD PSGRAVGVHQ 

    SAYK
    Length:554
    Mass (Da):62,659
    Last modified:January 23, 2007 - v3
    <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:i9091B269112C9F5C
    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
    		J05554 Genomic DNA Translation: AAA23498.1
    U00096 Genomic DNA Translation: AAC73768.1
    AP009048 Genomic DNA Translation: BAA35317.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A36616 AJECN

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415200.1, NC_000913.3
    WP_000337077.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73768; AAC73768; b0674
    BAA35317; BAA35317; BAA35317

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		945281

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0660
    eco:b0674

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1605

    <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
    		J05554 Genomic DNA Translation: AAA23498.1
    U00096 Genomic DNA Translation: AAC73768.1
    AP009048 Genomic DNA Translation: BAA35317.1
    PIRiA36616 AJECN
    RefSeqiNP_415200.1, NC_000913.3
    WP_000337077.1, 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
    1CT9X-ray2.00A/B/C/D2-554[»]
    ProteinModelPortaliP22106
    SMRiP22106
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261812, 416 interactors
    DIPiDIP-9177N
    IntActiP22106, 7 interactors
    STRINGi316385.ECDH10B_0739

    Protein family/group databases

    MEROPSiC44.976

    Proteomic databases

    EPDiP22106
    PaxDbiP22106
    PRIDEiP22106

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73768; AAC73768; b0674
    BAA35317; BAA35317; BAA35317
    GeneIDi945281
    KEGGiecj:JW0660
    eco:b0674
    PATRICifig|1411691.4.peg.1605

    Organism-specific databases

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

    More...    EchoBASEi    		EB0090
    EcoGeneiEG10092 asnB

    Phylogenomic databases

    eggNOGiENOG4105CAQ Bacteria
    COG0367 LUCA
    HOGENOMiHOG000027493
    InParanoidiP22106
    KOiK01953
    PhylomeDBiP22106

    Enzyme and pathway databases

    UniPathwayi
    UPA00134;UER00195

    BioCyciEcoCyc:ASNSYNB-MONOMER
    MetaCyc:ASNSYNB-MONOMER
    BRENDAi6.3.5.4 2026

    Miscellaneous databases

    EvolutionaryTraceiP22106

    Protein Ontology

    More...    PROi    		PR:P22106

    Family and domain databases

    CDDicd01991 Asn_Synthase_B_C, 1 hit
    cd00712 AsnB, 1 hit
    Gene3Di3.40.50.620, 1 hit
    3.60.20.10, 1 hit
    InterProiView protein in InterPro
    IPR006426 Asn_synth_AEB
    IPR001962 Asn_synthase
    IPR033738 AsnB_N
    IPR017932 GATase_2_dom
    IPR029055 Ntn_hydrolases_N
    IPR014729 Rossmann-like_a/b/a_fold
    PfamiView protein in Pfam
    PF00733 Asn_synthase, 1 hit
    PF13537 GATase_7, 1 hit
    PIRSFiPIRSF001589 Asn_synthetase_glu-h, 1 hit
    SUPFAMiSSF56235 SSF56235, 1 hit
    TIGRFAMsiTIGR01536 asn_synth_AEB, 1 hit
    PROSITEiView protein in PROSITE
    PS51278 GATASE_TYPE_2, 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 nameiASNB_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: P22106
    <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: August 1, 1991
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 158 of the entry and version 3 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, Direct protein sequencing, 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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