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P00805

- ASPG2_ECOLI

UniProt

P00805 - ASPG2_ECOLI

Protein

L-asparaginase 2

Gene

ansB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Kineticsi

    1. KM=0.115 µM for L-asparagine

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei34 – 341O-isoaspartyl threonine intermediate3 PublicationsPROSITE-ProRule annotation

    GO - Molecular functioni

    1. asparaginase activity Source: EcoCyc

    GO - Biological processi

    1. asparagine metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSB-MONOMER.
    ECOL316407:JW2924-MONOMER.
    MetaCyc:ANSB-MONOMER.
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10046. ansB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341T → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi111 – 1111T → S: Reduced enzyme activity. 1 Publication
    Mutagenesisi111 – 1111T → V: Loss of enzyme activity. 1 Publication

    Protein family/group databases

    Allergomei8365. Esc c Asparaginase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 348326L-asparaginase 2PRO_0000002356Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi99 ↔ 1272 Publications

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP00805.
    PRIDEiP00805.

    Expressioni

    Inductioni

    By cAMP and anaerobiosis.

    Gene expression databases

    GenevestigatoriP00805.

    Interactioni

    Subunit structurei

    Homotetramer.5 Publications

    Protein-protein interaction databases

    DIPiDIP-9110N.
    IntActiP00805. 7 interactions.
    STRINGi511145.b2957.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 339
    Helixi34 – 363
    Beta strandi42 – 443
    Beta strandi48 – 503
    Helixi54 – 596
    Helixi62 – 665
    Beta strandi69 – 7810
    Helixi80 – 823
    Helixi85 – 9814
    Helixi99 – 1013
    Beta strandi103 – 1086
    Beta strandi111 – 1133
    Helixi114 – 12411
    Beta strandi131 – 1344
    Helixi147 – 15913
    Helixi161 – 1633
    Beta strandi168 – 1725
    Beta strandi175 – 1784
    Turni179 – 1813
    Beta strandi182 – 1843
    Beta strandi186 – 1883
    Beta strandi193 – 1953
    Turni196 – 1983
    Beta strandi201 – 2055
    Beta strandi208 – 2114
    Helixi220 – 2223
    Beta strandi236 – 2405
    Helixi248 – 2558
    Beta strandi259 – 2668
    Turni267 – 2693
    Helixi273 – 28412
    Beta strandi288 – 29811
    Beta strandi302 – 3065
    Helixi308 – 3114
    Beta strandi313 – 3153
    Helixi321 – 33111
    Turni332 – 3343
    Helixi338 – 3458

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 23-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00805.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni80 – 812Substrate binding
    Regioni111 – 1122Substrate binding

    Sequence similaritiesi

    Belongs to the asparaginase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0252.
    HOGENOMiHOG000044165.
    KOiK01424.
    OMAiADISGEQ.
    OrthoDBiEOG6VTK47.
    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00805-1 [UniParc]FASTAAdd to Basket

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    MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG    50
    KVGVENLVNA VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD 100
    KTDGFVITHG TDTMEETAYF LDLTVKCDKP VVMVGAMRPS TSMSADGPFN 150
    LYNAVVTAAD KASANRGVLV VMNDTVLDGR DVTKTNTTDV ATFKSVNYGP 200
    LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY NYANASDLPA 250
    KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT 300
    TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY 348
    Length:348
    Mass (Da):36,851
    Last modified:November 1, 1990 - v2
    Checksum:i2076987C0E8B2F99
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491V → A AA sequence (PubMed:6766894)Curated
    Sequence conflicti86 – 861N → D AA sequence (PubMed:6766894)Curated
    Sequence conflicti132 – 1321Missing AA sequence (PubMed:6766894)Curated
    Sequence conflicti156 – 1561Missing AA sequence (PubMed:6766894)Curated
    Sequence conflicti171 – 1711Missing AA sequence (PubMed:6766894)Curated
    Sequence conflicti206 – 2061N → D AA sequence (PubMed:6766894)Curated
    Sequence conflicti268 – 2681N → D AA sequence (PubMed:6766894)Curated
    Sequence conflicti274 – 2741S → T AA sequence (PubMed:6766894)Curated
    Sequence conflicti285 – 2851T → D AA sequence (PubMed:6766894)Curated
    Sequence conflicti290 – 2901Missing AA sequence (PubMed:6766894)Curated
    Sequence conflicti330 – 3301Missing AA sequence (PubMed:6766894)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491156.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75994; AAC75994; b2957.
    BAE77020; BAE77020; BAE77020.
    GeneIDi12930249.
    947454.
    KEGGiecj:Y75_p2887.
    eco:b2957.
    PATRICi32121326. VBIEscCol129921_3051.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A35132. XDEC.
    RefSeqi NP_417432.1. NC_000913.3.
    YP_491156.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HO3 X-ray 2.50 A/B 23-348 [» ]
    1IHD X-ray 2.65 A/C 23-348 [» ]
    1JAZ X-ray 2.27 A/B 23-348 [» ]
    1JJA X-ray 2.30 A/B/C/D/E/F 23-348 [» ]
    1NNS X-ray 1.95 A/B 23-348 [» ]
    3ECA X-ray 2.40 A/B/C/D 23-348 [» ]
    4ECA X-ray 2.20 A/B/C/D 23-348 [» ]
    ProteinModelPortali P00805.
    SMRi P00805. Positions 23-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9110N.
    IntActi P00805. 7 interactions.
    STRINGi 511145.b2957.

    Protein family/group databases

    Allergomei 8365. Esc c Asparaginase.

    Proteomic databases

    PaxDbi P00805.
    PRIDEi P00805.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75994 ; AAC75994 ; b2957 .
    BAE77020 ; BAE77020 ; BAE77020 .
    GeneIDi 12930249.
    947454.
    KEGGi ecj:Y75_p2887.
    eco:b2957.
    PATRICi 32121326. VBIEscCol129921_3051.

    Organism-specific databases

    EchoBASEi EB0044.
    EcoGenei EG10046. ansB.

    Phylogenomic databases

    eggNOGi COG0252.
    HOGENOMi HOG000044165.
    KOi K01424.
    OMAi ADISGEQ.
    OrthoDBi EOG6VTK47.
    PhylomeDBi P00805.

    Enzyme and pathway databases

    BioCyci EcoCyc:ANSB-MONOMER.
    ECOL316407:JW2924-MONOMER.
    MetaCyc:ANSB-MONOMER.
    SABIO-RK P00805.

    Miscellaneous databases

    EvolutionaryTracei P00805.
    PROi P00805.

    Gene expression databases

    Genevestigatori P00805.

    Family and domain databases

    Gene3Di 3.40.50.1170. 1 hit.
    3.40.50.40. 1 hit.
    InterProi IPR004550. AsnASE_II.
    IPR006034. Asparaginase/glutaminase.
    IPR020827. Asparaginase/glutaminase_AS1.
    IPR027475. Asparaginase/glutaminase_AS2.
    IPR027473. L-asparaginase_C.
    IPR027474. L-asparaginase_N.
    [Graphical view ]
    Pfami PF00710. Asparaginase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001220. L-ASNase_gatD. 1 hit.
    PRINTSi PR00139. ASNGLNASE.
    SMARTi SM00870. Asparaginase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53774. SSF53774. 1 hit.
    TIGRFAMsi TIGR00520. asnASE_II. 1 hit.
    PROSITEi PS00144. ASN_GLN_ASE_1. 1 hit.
    PS00917. ASN_GLN_ASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins."
      Jennings M.P., Beacham I.R.
      J. Bacteriol. 172:1491-1498(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene."
      Bonthron D.T.
      Gene 91:101-105(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "The primary structure of L-asparaginase from Escherichia coli."
      Maita T., Matsuda G.
      Hoppe-Seyler's Z. Physiol. Chem. 361:105-117(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-348.
    6. "Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli."
      Maita T., Morokuma K., Matsuda G.
      Hoppe-Seyler's Z. Physiol. Chem. 360:1483-1495(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    7. "Structure of peptide from active site region of Escherichia coli L-asparaginase."
      Peterson R.G., Richards F.F., Handschumacher R.E.
      J. Biol. Chem. 252:2072-2076(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    8. "Chemical evidence for identical subunits in L-asparaginase from Escherichia coli B."
      Greenquist A.C., Wriston J.C. Jr.
      Arch. Biochem. Biophys. 152:280-286(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis."
      Harms E., Wehner A., Aung H.P., Roehm K.H.
      FEBS Lett. 285:55-58(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE THR-34, MUTAGENESIS OF THR-34, SUBUNIT.
    10. "Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis."
      Wehner A., Harms E., Jennings M.P., Beacham I.R., Derst C., Bast P., Roehm K.H.
      Eur. J. Biochem. 208:475-480(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HISTIDINE RESIDUES.
    11. "Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis."
      Ders C., Henseling J., Roehm K.H.
      Protein Eng. 5:785-789(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THREONINE AND SERINE RESIDUES.
    12. "Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy."
      Swain A.L., Jaskolski M., Housset D., Rao J.K.M., Wlodawer A.
      Proc. Natl. Acad. Sci. U.S.A. 90:1474-1478(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ASPARTIC ACID, DISULFIDE BOND, SUBUNIT.
    13. "A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant."
      Palm G.J., Lubkowski J., Derst C., Schleper S., Roehm K.H., Wlodawer A.
      FEBS Lett. 390:211-216(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT VAL-111, ACTIVE SITE, MUTAGENESIS OF THR-111, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BOND.
    14. "Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups."
      Sanches M., Barbosa J.A., de Oliveira R.T., Abrahao Neto J., Polikarpov I.
      Acta Crystallogr. D 59:416-422(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 23-348 IN COMPLEXES WITH ASPARTIC ACID, SUBUNIT.

    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: October 1, 2014
    This is version 147 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

    External Data

    Dasty 3