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 - P00805 (ASPG2_ECOLI)

Entry version 177 (05 Jun 2019)
Sequence version 2 (01 Nov 1990)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

L-asparaginase 2

Gene

ansB

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

Miscellaneous

E.coli contains two L-asparaginase isoenzymes: L-asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-asparaginase II, a high-affinity secreted enzyme.

<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 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=0.115 µM for L-asparagine

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei34O-isoaspartyl threonine intermediatePROSITE-ProRule 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

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:ANSB-MONOMER
    ECOL316407:JW2924-MONOMER
    MetaCyc:ANSB-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.5.1.1 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P00805

    <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:
    L-asparaginase 2 (EC:3.5.1.1)
    Alternative name(s):
    L-asparaginase II
    Short name:
    L-ASNase II
    L-asparagine amidohydrolase II
    INN: Colaspase
    <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:ansB
    Ordered Locus Names:b2957, JW2924
    <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    		EG10046 ansB

    <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 ...

    Keywords - Cellular componenti

    Periplasm

    <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 use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

    Available under the names Crastinin (Bayer), Elspar (Merck), Kidrolase (Rhone-Poulenc) and Leunase (Kyowa). Also available as a PEG-conjugated form (Pegaspargase) under the name Oncaspar (Enzon). Used as an antineoplastic in chemotherapy. Reduces the quantity of asparagine available to cancer cells.

    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>Mutagenesisi34T → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi111T → S: Reduced enzyme activity. 1 Publication1
    Mutagenesisi111T → V: Loss of enzyme activity. 1 Publication1

    Protein family/group databases

    Allergome; a platform for allergen knowledge

    More...    Allergomei    		8365 Esc c Asparaginase

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB01817 Threonine-Aspartic Ester

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 221 PublicationAdd BLAST22
    <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_000000235623 – 348L-asparaginase 2Add BLAST326

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi99 ↔ 1272 Publications

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P00805

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

    More...    PaxDbi    		P00805

    PRoteomics IDEntifications database

    More...    PRIDEi    		P00805

    <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 cAMP and anaerobiosis.

    <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

    Homotetramer.

    5 Publications

    <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
    itself2EBI-907458,EBI-907458

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4259243, 267 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-9110N

    Protein interaction database and analysis system

    More...    IntActi    		P00805, 8 interactors

    Molecular INTeraction database

    More...    MINTi    		P00805

    STRING: functional protein association networks

    More...    STRINGi    		511145.b2957

    <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

    1348
    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    		P00805

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P00805

    <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>Domaini24 – 348Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST325

    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>Regioni80 – 81Substrate binding2
    Regioni111 – 112Substrate binding2

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the asparaginase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105HDK Bacteria
    COG0252 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000044165

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P00805

    KEGG Orthology (KO)

    More...    KOi    		K01424

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P00805

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.1170, 1 hit
    3.40.50.40, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR004550 AsnASE_II
    IPR036152 Asp/glu_Ase-like_sf
    IPR006034 Asparaginase/glutaminase-like
    IPR020827 Asparaginase/glutaminase_AS1
    IPR027475 Asparaginase/glutaminase_AS2
    IPR040919 Asparaginase_C
    IPR027473 L-asparaginase_C
    IPR027474 L-asparaginase_N
    IPR037152 L-asparaginase_N_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00710 Asparaginase, 1 hit
    PF17763 Asparaginase_C, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001220 L-ASNase_gatD, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00139 ASNGLNASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00870 Asparaginase, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF53774 SSF53774, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00520 asnASE_II, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00144 ASN_GLN_ASE_1, 1 hit
    PS00917 ASN_GLN_ASE_2, 1 hit
    PS51732 ASN_GLN_ASE_3, 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>. 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_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.

    P00805-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG 
            60         70         80         90        100
    KVGVENLVNA VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD 
           110        120        130        140        150
    KTDGFVITHG TDTMEETAYF LDLTVKCDKP VVMVGAMRPS TSMSADGPFN 
           160        170        180        190        200
    LYNAVVTAAD KASANRGVLV VMNDTVLDGR DVTKTNTTDV ATFKSVNYGP 
           210        220        230        240        250
    LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY NYANASDLPA 
           260        270        280        290        300
    KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT 
           310        320        330        340 
    TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY
    Length:348
    Mass (Da):36,851
    Last modified:November 1, 1990 - v2
    <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:i2076987C0E8B2F99
    GO

    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 conflicti49V → A AA sequence (PubMed:6766894).Curated1
    Sequence conflicti86N → D AA sequence (PubMed:6766894).Curated1
    Sequence conflicti132Missing AA sequence (PubMed:6766894).Curated1
    Sequence conflicti156Missing AA sequence (PubMed:6766894).Curated1
    Sequence conflicti171Missing AA sequence (PubMed:6766894).Curated1
    Sequence conflicti206N → D AA sequence (PubMed:6766894).Curated1
    Sequence conflicti268N → D AA sequence (PubMed:6766894).Curated1
    Sequence conflicti274S → T AA sequence (PubMed:6766894).Curated1
    Sequence conflicti285T → D AA sequence (PubMed:6766894).Curated1
    Sequence conflicti290Missing AA sequence (PubMed:6766894).Curated1
    Sequence conflicti330Missing AA sequence (PubMed:6766894).Curated1

    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
    		M34277 Genomic DNA Translation: AAA24062.1
    M34234 Genomic DNA Translation: AAA23445.1
    U28377 Genomic DNA Translation: AAA69124.1
    U00096 Genomic DNA Translation: AAC75994.1
    AP009048 Genomic DNA Translation: BAE77020.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A35132 XDEC

    NCBI Reference Sequences

    More...    RefSeqi    		NP_417432.1, NC_000913.3
    WP_000394140.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC75994; AAC75994; b2957
    BAE77020; BAE77020; BAE77020

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		947454

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW2924
    eco:b2957

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.3775

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		M34277 Genomic DNA Translation: AAA24062.1
    M34234 Genomic DNA Translation: AAA23445.1
    U28377 Genomic DNA Translation: AAA69124.1
    U00096 Genomic DNA Translation: AAC75994.1
    AP009048 Genomic DNA Translation: BAE77020.1
    PIRiA35132 XDEC
    RefSeqiNP_417432.1, NC_000913.3
    WP_000394140.1, 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
    1HO3X-ray2.50A/B23-348[»]
    1IHDX-ray2.65A/C23-348[»]
    1JAZX-ray2.27A/B23-348[»]
    1JJAX-ray2.30A/B/C/D/E/F23-348[»]
    1NNSX-ray1.95A/B23-348[»]
    3ECAX-ray2.40A/B/C/D23-348[»]
    4ECAX-ray2.20A/B/C/D23-348[»]
    5MQ5X-ray1.60A/B/C/D23-348[»]
    6EOKX-ray2.50A/B/C/D23-348[»]
    SMRiP00805
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4259243, 267 interactors
    DIPiDIP-9110N
    IntActiP00805, 8 interactors
    MINTiP00805
    STRINGi511145.b2957

    Chemistry databases

    DrugBankiDB01817 Threonine-Aspartic Ester

    Protein family/group databases

    Allergomei8365 Esc c Asparaginase

    Proteomic databases

    jPOSTiP00805
    PaxDbiP00805
    PRIDEiP00805

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75994; AAC75994; b2957
    BAE77020; BAE77020; BAE77020
    GeneIDi947454
    KEGGiecj:JW2924
    eco:b2957
    PATRICifig|1411691.4.peg.3775

    Organism-specific databases

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

    More...    EchoBASEi    		EB0044
    EcoGeneiEG10046 ansB

    Phylogenomic databases

    eggNOGiENOG4105HDK Bacteria
    COG0252 LUCA
    HOGENOMiHOG000044165
    InParanoidiP00805
    KOiK01424
    PhylomeDBiP00805

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSB-MONOMER
    ECOL316407:JW2924-MONOMER
    MetaCyc:ANSB-MONOMER
    BRENDAi3.5.1.1 2026
    SABIO-RKiP00805

    Miscellaneous databases

    EvolutionaryTraceiP00805

    Protein Ontology

    More...    PROi    		PR:P00805

    Family and domain databases

    Gene3Di3.40.50.1170, 1 hit
    3.40.50.40, 1 hit
    InterProiView protein in InterPro
    IPR004550 AsnASE_II
    IPR036152 Asp/glu_Ase-like_sf
    IPR006034 Asparaginase/glutaminase-like
    IPR020827 Asparaginase/glutaminase_AS1
    IPR027475 Asparaginase/glutaminase_AS2
    IPR040919 Asparaginase_C
    IPR027473 L-asparaginase_C
    IPR027474 L-asparaginase_N
    IPR037152 L-asparaginase_N_sf
    PfamiView protein in Pfam
    PF00710 Asparaginase, 1 hit
    PF17763 Asparaginase_C, 1 hit
    PIRSFiPIRSF001220 L-ASNase_gatD, 1 hit
    PRINTSiPR00139 ASNGLNASE
    SMARTiView protein in SMART
    SM00870 Asparaginase, 1 hit
    SUPFAMiSSF53774 SSF53774, 1 hit
    TIGRFAMsiTIGR00520 asnASE_II, 1 hit
    PROSITEiView protein in PROSITE
    PS00144 ASN_GLN_ASE_1, 1 hit
    PS00917 ASN_GLN_ASE_2, 1 hit
    PS51732 ASN_GLN_ASE_3, 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 nameiASPG2_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: P00805
    Secondary accession number(s): Q2M9N6
    <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: July 21, 1986
    Last sequence update: November 1, 1990
    Last modified: June 5, 2019
    This is version 177 of the entry and version 2 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, Pharmaceutical, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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