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Protein

L-asparaginase 2

Gene

ansB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.1 Publication

Kineticsi

  1. KM=0.115 µM for L-asparagine

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei34O-isoaspartyl threonine intermediatePROSITE-ProRule annotation1 Publication1

    GO - Molecular functioni

    • asparaginase activity Source: EcoCyc

    GO - Biological processi

    • asparagine catabolic process Source: GO_Central
    • protein homotetramerization Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSB-MONOMER.
    ECOL316407:JW2924-MONOMER.
    MetaCyc:ANSB-MONOMER.
    BRENDAi3.5.1.1. 2026.
    SABIO-RKP00805.

    Names & Taxonomyi

    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
    Gene namesi
    Name:ansB
    Ordered Locus Names:b2957, JW2924
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10046. ansB.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • outer membrane-bounded periplasmic space Source: EcoCyc
    • periplasmic space Source: EcoliWiki
    Complete GO annotation...

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    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
    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

    Allergomei8365. Esc c Asparaginase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 221 PublicationAdd BLAST22
    ChainiPRO_000000235623 – 348L-asparaginase 2Add BLAST326

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi99 ↔ 1272 Publications

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP00805.
    PRIDEiP00805.

    Expressioni

    Inductioni

    By cAMP and anaerobiosis.

    Interactioni

    Subunit structurei

    Homotetramer.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-907458,EBI-907458

    Protein-protein interaction databases

    BioGridi4259243. 248 interactors.
    DIPiDIP-9110N.
    IntActiP00805. 7 interactors.
    STRINGi511145.b2957.

    Structurei

    Secondary structure

    1348
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi25 – 33Combined sources9
    Helixi34 – 36Combined sources3
    Beta strandi42 – 44Combined sources3
    Beta strandi48 – 50Combined sources3
    Helixi54 – 59Combined sources6
    Helixi62 – 66Combined sources5
    Beta strandi69 – 78Combined sources10
    Helixi80 – 82Combined sources3
    Helixi85 – 98Combined sources14
    Helixi99 – 101Combined sources3
    Beta strandi103 – 108Combined sources6
    Beta strandi111 – 113Combined sources3
    Helixi114 – 124Combined sources11
    Beta strandi131 – 134Combined sources4
    Helixi147 – 159Combined sources13
    Helixi161 – 163Combined sources3
    Beta strandi168 – 172Combined sources5
    Beta strandi175 – 178Combined sources4
    Turni179 – 181Combined sources3
    Beta strandi182 – 184Combined sources3
    Beta strandi186 – 188Combined sources3
    Beta strandi193 – 195Combined sources3
    Turni196 – 198Combined sources3
    Beta strandi201 – 205Combined sources5
    Beta strandi208 – 211Combined sources4
    Helixi220 – 222Combined sources3
    Beta strandi236 – 240Combined sources5
    Helixi248 – 255Combined sources8
    Beta strandi259 – 266Combined sources8
    Turni267 – 269Combined sources3
    Helixi273 – 284Combined sources12
    Beta strandi288 – 298Combined sources11
    Beta strandi302 – 306Combined sources5
    Helixi308 – 311Combined sources4
    Beta strandi313 – 315Combined sources3
    Helixi321 – 331Combined sources11
    Turni332 – 334Combined sources3
    Helixi338 – 345Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP00805.
    SMRiP00805.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00805.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini24 – 348Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST325

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni80 – 81Substrate binding2
    Regioni111 – 112Substrate binding2

    Sequence similaritiesi

    Belongs to the asparaginase 1 family.Curated
    Contains 1 asparaginase/glutaminase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105HDK. Bacteria.
    COG0252. LUCA.
    HOGENOMiHOG000044165.
    InParanoidiP00805.
    KOiK01424.
    OMAiNFGPLGY.
    PhylomeDBiP00805.

    Family and domain databases

    Gene3Di3.40.50.1170. 1 hit.
    3.40.50.40. 1 hit.
    InterProiIPR004550. AsnASE_II.
    IPR006034. Asparaginase/glutaminase.
    IPR020827. Asparaginase/glutaminase_AS1.
    IPR027475. Asparaginase/glutaminase_AS2.
    IPR027473. L-asparaginase_C.
    IPR027474. L-asparaginase_N.
    [Graphical view]
    PfamiPF00710. Asparaginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
    PRINTSiPR00139. ASNGLNASE.
    SMARTiSM00870. Asparaginase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53774. SSF53774. 1 hit.
    TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
    PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
    PS00917. ASN_GLN_ASE_2. 1 hit.
    PS51732. ASN_GLN_ASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    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
    Checksum:i2076987C0E8B2F99
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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:
    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.

    Genome annotation databases

    EnsemblBacteriaiAAC75994; AAC75994; b2957.
    BAE77020; BAE77020; BAE77020.
    GeneIDi947454.
    KEGGiecj:JW2924.
    eco:b2957.
    PATRICi32121326. VBIEscCol129921_3051.

    Cross-referencesi

    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:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP00805.
    SMRiP00805.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259243. 248 interactors.
    DIPiDIP-9110N.
    IntActiP00805. 7 interactors.
    STRINGi511145.b2957.

    Protein family/group databases

    Allergomei8365. Esc c Asparaginase.

    Proteomic databases

    PaxDbiP00805.
    PRIDEiP00805.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75994; AAC75994; b2957.
    BAE77020; BAE77020; BAE77020.
    GeneIDi947454.
    KEGGiecj:JW2924.
    eco:b2957.
    PATRICi32121326. VBIEscCol129921_3051.

    Organism-specific databases

    EchoBASEiEB0044.
    EcoGeneiEG10046. ansB.

    Phylogenomic databases

    eggNOGiENOG4105HDK. Bacteria.
    COG0252. LUCA.
    HOGENOMiHOG000044165.
    InParanoidiP00805.
    KOiK01424.
    OMAiNFGPLGY.
    PhylomeDBiP00805.

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSB-MONOMER.
    ECOL316407:JW2924-MONOMER.
    MetaCyc:ANSB-MONOMER.
    BRENDAi3.5.1.1. 2026.
    SABIO-RKP00805.

    Miscellaneous databases

    EvolutionaryTraceiP00805.
    PROiP00805.

    Family and domain databases

    Gene3Di3.40.50.1170. 1 hit.
    3.40.50.40. 1 hit.
    InterProiIPR004550. AsnASE_II.
    IPR006034. Asparaginase/glutaminase.
    IPR020827. Asparaginase/glutaminase_AS1.
    IPR027475. Asparaginase/glutaminase_AS2.
    IPR027473. L-asparaginase_C.
    IPR027474. L-asparaginase_N.
    [Graphical view]
    PfamiPF00710. Asparaginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
    PRINTSiPR00139. ASNGLNASE.
    SMARTiSM00870. Asparaginase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53774. SSF53774. 1 hit.
    TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
    PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
    PS00917. ASN_GLN_ASE_2. 1 hit.
    PS51732. ASN_GLN_ASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiASPG2_ECOLI
    AccessioniPrimary (citable) accession number: P00805
    Secondary accession number(s): Q2M9N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1990
    Last modified: November 2, 2016
    This is version 160 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.