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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)DescriptionActionsGraphical viewLength
    Active sitei14O-isoaspartyl threonine intermediatePROSITE-ProRule annotation1 Publication1
    Binding sitei162Allosteric activator1
    Binding sitei240Allosteric activator1

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi14T → A or V: Loss of enzyme activity. 1 Publication1
    Mutagenesisi61S → Q: Loss of enzyme activity. 1
    Mutagenesisi91T → A or V: Loss of enzyme activity. 1 Publication1
    Mutagenesisi118Q → D: Loss of enzyme activity. 1 Publication1
    Mutagenesisi162T → A: No effect on activity at saturating substrate concentration. Abolishes cooperativity. 1 Publication1
    Mutagenesisi240R → A: No effect on activity at saturating substrate concentration. Reduced activity at lower substrate concentrations. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001710791 – 338L-asparaginase 1Add BLAST338

    Proteomic databases

    PaxDbiP0A962.
    PRIDEiP0A962.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 13Combined sources9
    Helixi14 – 16Combined sources3
    Beta strandi18 – 20Combined sources3
    Beta strandi23 – 25Combined sources3
    Helixi30 – 35Combined sources6
    Helixi39 – 42Combined sources4
    Beta strandi48 – 58Combined sources11
    Helixi60 – 62Combined sources3
    Helixi65 – 78Combined sources14
    Helixi79 – 81Combined sources3
    Beta strandi83 – 88Combined sources6
    Helixi94 – 104Combined sources11
    Beta strandi105 – 107Combined sources3
    Beta strandi112 – 115Combined sources4
    Beta strandi123 – 125Combined sources3
    Helixi128 – 141Combined sources14
    Beta strandi145 – 151Combined sources7
    Beta strandi154 – 157Combined sources4
    Helixi158 – 160Combined sources3
    Beta strandi162 – 165Combined sources4
    Beta strandi168 – 170Combined sources3
    Beta strandi171 – 173Combined sources3
    Beta strandi180 – 189Combined sources10
    Beta strandi199 – 201Combined sources3
    Beta strandi212 – 216Combined sources5
    Helixi224 – 229Combined sources6
    Beta strandi231 – 233Combined sources3
    Beta strandi235 – 242Combined sources8
    Turni243 – 245Combined sources3
    Helixi251 – 262Combined sources12
    Beta strandi266 – 275Combined sources10
    Helixi288 – 291Combined sources4
    Helixi302 – 314Combined sources13
    Helixi319 – 326Combined sources8
    Beta strandi330 – 334Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A962.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 329Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST326

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni59 – 61Substrate binding3
    Regioni91 – 92Substrate binding2
    Regioni271 – 273Allosteric activator binding3

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259141. 6 interactors.
    DIPiDIP-9109N.
    IntActiP0A962. 6 interactors.
    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: November 2, 2016
    This is version 96 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.