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Protein

L-asparaginase 1

Gene

ansA

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

Enzyme regulationi

Shows cooperative activation. Allosterically activated by asparagine.1 Publication

Kineticsi

  1. KM=3.5 mM for L-asparagine

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei14 – 141O-isoaspartyl threonine intermediatePROSITE-ProRule annotation1 Publication
    Binding sitei162 – 1621Allosteric activator
    Binding sitei240 – 2401Allosteric activator

    GO - Molecular functioni

    • asparaginase activity Source: EcoCyc
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    • asparagine catabolic process via L-aspartate Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSA-MONOMER.
    ECOL316407:JW1756-MONOMER.
    MetaCyc:ANSA-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-asparaginase 1 (EC:3.5.1.1)
    Alternative name(s):
    L-asparaginase I
    Short name:
    L-ASNase I
    L-asparagine amidohydrolase I
    Gene namesi
    Name:ansA
    Ordered Locus Names:b1767, JW1756
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10045. ansA.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoCyc
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141T → A or V: Loss of enzyme activity. 1 Publication
    Mutagenesisi61 – 611S → Q: Loss of enzyme activity.
    Mutagenesisi91 – 911T → A or V: Loss of enzyme activity. 1 Publication
    Mutagenesisi118 – 1181Q → D: Loss of enzyme activity. 1 Publication
    Mutagenesisi162 – 1621T → A: No effect on activity at saturating substrate concentration. Abolishes cooperativity. 1 Publication
    Mutagenesisi240 – 2401R → A: No effect on activity at saturating substrate concentration. Reduced activity at lower substrate concentrations. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 338338L-asparaginase 1PRO_0000171079Add
    BLAST

    Proteomic databases

    PaxDbiP0A962.
    PRIDEiP0A962.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4259141. 6 interactions.
    DIPiDIP-9109N.
    IntActiP0A962. 6 interactions.
    STRINGi511145.b1767.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139Combined sources
    Helixi14 – 163Combined sources
    Beta strandi18 – 203Combined sources
    Beta strandi23 – 253Combined sources
    Helixi30 – 356Combined sources
    Helixi39 – 424Combined sources
    Beta strandi48 – 5811Combined sources
    Helixi60 – 623Combined sources
    Helixi65 – 7814Combined sources
    Helixi79 – 813Combined sources
    Beta strandi83 – 886Combined sources
    Helixi94 – 10411Combined sources
    Beta strandi105 – 1073Combined sources
    Beta strandi112 – 1154Combined sources
    Beta strandi123 – 1253Combined sources
    Helixi128 – 14114Combined sources
    Beta strandi145 – 1517Combined sources
    Beta strandi154 – 1574Combined sources
    Helixi158 – 1603Combined sources
    Beta strandi162 – 1654Combined sources
    Beta strandi168 – 1703Combined sources
    Beta strandi171 – 1733Combined sources
    Beta strandi180 – 18910Combined sources
    Beta strandi199 – 2013Combined sources
    Beta strandi212 – 2165Combined sources
    Helixi224 – 2296Combined sources
    Beta strandi231 – 2333Combined sources
    Beta strandi235 – 2428Combined sources
    Turni243 – 2453Combined sources
    Helixi251 – 26212Combined sources
    Beta strandi266 – 27510Combined sources
    Helixi288 – 2914Combined sources
    Helixi302 – 31413Combined sources
    Helixi319 – 3268Combined sources
    Beta strandi330 – 3345Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HIMX-ray1.82A/B/C/D1-338[»]
    2P2DX-ray1.89A/B/C/D1-338[»]
    2P2NX-ray1.90A/B/C/D1-338[»]
    ProteinModelPortaliP0A962.
    SMRiP0A962. Positions 2-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A962.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 329326Asparaginase/glutaminasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 613Substrate binding
    Regioni91 – 922Substrate binding
    Regioni271 – 2733Allosteric activator binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105HDK. Bacteria.
    COG0252. LUCA.
    HOGENOMiHOG000227974.
    InParanoidiP0A962.
    KOiK01424.
    OMAiMPEFYHD.
    PhylomeDBiP0A962.

    Family and domain databases

    Gene3Di3.40.50.1170. 1 hit.
    3.40.50.40. 1 hit.
    InterProiIPR006033. AsnASEI.
    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.
    TIGRFAMsiTIGR00519. asnASE_I. 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.

    P0A962-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQKKSIYVAY TGGTIGMQRS EQGYIPVSGH LQRQLALMPE FHRPEMPDFT
    60 70 80 90 100
    IHEYTPLMDS SDMTPEDWQH IAEDIKAHYD DYDGFVILHG TDTMAYTASA
    110 120 130 140 150
    LSFMLENLGK PVIVTGSQIP LAELRSDGQI NLLNALYVAA NYPINEVTLF
    160 170 180 190 200
    FNNRLYRGNR TTKAHADGFD AFASPNLPPL LEAGIHIRRL NTPPAPHGEG
    210 220 230 240 250
    ELIVHPITPQ PIGVVTIYPG ISADVVRNFL RQPVKALILR SYGVGNAPQN
    260 270 280 290 300
    KAFLQELQEA SDRGIVVVNL TQCMSGKVNM GGYATGNALA HAGVIGGADM
    310 320 330
    TVEATLTKLH YLLSQELDTE TIRKAMSQNL RGELTPDD
    Length:338
    Mass (Da):37,127
    Last modified:July 19, 2005 - v1
    Checksum:i75D97E6D10E9F8DA
    GO

    Sequence cautioni

    The sequence AAA23446 differs from that shown. Reason: Erroneous initiation. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26934 Genomic DNA. Translation: AAA23446.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC74837.1.
    AP009048 Genomic DNA. Translation: BAA15558.1.
    PIRiG64936. XDEC1.
    RefSeqiNP_416281.1. NC_000913.3.
    WP_001170162.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74837; AAC74837; b1767.
    BAA15558; BAA15558; BAA15558.
    GeneIDi946278.
    KEGGiecj:JW1756.
    eco:b1767.
    PATRICi32118845. VBIEscCol129921_1840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M26934 Genomic DNA. Translation: AAA23446.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC74837.1.
    AP009048 Genomic DNA. Translation: BAA15558.1.
    PIRiG64936. XDEC1.
    RefSeqiNP_416281.1. NC_000913.3.
    WP_001170162.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HIMX-ray1.82A/B/C/D1-338[»]
    2P2DX-ray1.89A/B/C/D1-338[»]
    2P2NX-ray1.90A/B/C/D1-338[»]
    ProteinModelPortaliP0A962.
    SMRiP0A962. Positions 2-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259141. 6 interactions.
    DIPiDIP-9109N.
    IntActiP0A962. 6 interactions.
    STRINGi511145.b1767.

    Proteomic databases

    PaxDbiP0A962.
    PRIDEiP0A962.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74837; AAC74837; b1767.
    BAA15558; BAA15558; BAA15558.
    GeneIDi946278.
    KEGGiecj:JW1756.
    eco:b1767.
    PATRICi32118845. VBIEscCol129921_1840.

    Organism-specific databases

    EchoBASEiEB0043.
    EcoGeneiEG10045. ansA.

    Phylogenomic databases

    eggNOGiENOG4105HDK. Bacteria.
    COG0252. LUCA.
    HOGENOMiHOG000227974.
    InParanoidiP0A962.
    KOiK01424.
    OMAiMPEFYHD.
    PhylomeDBiP0A962.

    Enzyme and pathway databases

    BioCyciEcoCyc:ANSA-MONOMER.
    ECOL316407:JW1756-MONOMER.
    MetaCyc:ANSA-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A962.
    PROiP0A962.

    Family and domain databases

    Gene3Di3.40.50.1170. 1 hit.
    3.40.50.40. 1 hit.
    InterProiIPR006033. AsnASEI.
    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.
    TIGRFAMsiTIGR00519. asnASE_I. 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 nameiASPG1_ECOLI
    AccessioniPrimary (citable) accession number: P0A962
    Secondary accession number(s): P18840
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: September 7, 2016
    This is version 95 of the entry and version 1 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, Allosteric enzyme, Complete proteome, 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.