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Protein

L-asparaginase 2

Gene

ansB

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

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.

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
    • identical protein binding Source: IntAct

    GO - Biological processi

    • asparagine catabolic process Source: GO_Central
    • protein homotetramerization Source: EcoCyc

    Keywordsi

    Molecular functionHydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSB-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

    • outer membrane-bounded periplasmic space Source: EcoCyc

    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

    Chemistry databases

    DrugBankiDB01817 Threonine-Aspartic Ester

    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

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4259243, 267 interactors
    DIPiDIP-9110N
    IntActiP00805, 8 interactors
    MINTiP00805
    STRINGi316385.ECDH10B_3132

    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 – 283Combined sources11
    Turni284 – 286Combined sources3
    Beta strandi288 – 298Combined sources11
    Beta strandi302 – 306Combined sources5
    Helixi308 – 311Combined sources4
    Beta strandi313 – 315Combined sources3
    Helixi321 – 331Combined sources11
    Turni332 – 334Combined sources3
    Helixi338 – 347Combined sources10

    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[»]
    5MQ5X-ray1.60A/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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105HDK Bacteria
    COG0252 LUCA
    HOGENOMiHOG000044165
    InParanoidiP00805
    KOiK01424
    OMAiNVYSTGR
    PhylomeDBiP00805

    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
    IPR027473 L-asparaginase_C
    IPR027474 L-asparaginase_N
    IPR037152 L-asparaginase_N_sf
    PfamiView protein in Pfam
    PF00710 Asparaginase, 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

    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
    PATRICifig|1411691.4.peg.3775

    Similar proteinsi

    Entry informationi

    Entry nameiASPG2_ECOLI
    AccessioniPrimary (citable) accession number: P00805
    Secondary accession number(s): Q2M9N6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1990
    Last modified: April 25, 2018
    This is version 170 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

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