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P0CX79

- ASP24_YEAST

UniProt

P0CX79 - ASP24_YEAST

Protein

L-asparaginase 2-4

Gene

ASP3-4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Kineticsi

    Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine.

    1. KM=0.27 mM for L-asparagine2 Publications
    2. KM=0.27 mM for D-asparagine2 Publications
    3. KM=0.27 mM for N-acetyl-L-asparagine2 Publications
    4. KM=0.07 mM for N-carbamyl-L-asparagine2 Publications
    5. KM=0.06 mM for N-isoleucyl-L-asparagine2 Publications
    6. KM=0.06 mM for N-glycyl-L-asparagine2 Publications
    7. KM=0.06 mM for N-valyl-L-asparagine2 Publications
    8. KM=0.2 mM for N-methionyl-L-asparagine2 Publications
    9. KM=0.4 mM for N-glycyl-D-asparagine2 Publications

    Vmax=42 µmol/min/mg enzyme for L-asparagine2 Publications

    Vmax=60 µmol/min/mg enzyme for D-asparagine2 Publications

    Vmax=167 µmol/min/mg enzyme for N-acetyl-L-asparagine2 Publications

    Vmax=79 µmol/min/mg enzyme for N-carbamyl-L-asparagine2 Publications

    Vmax=67 µmol/min/mg enzyme for N-isoleucyl-L-asparagine2 Publications

    Vmax=135 µmol/min/mg enzyme for N-glycyl-L-asparagine2 Publications

    Vmax=56 µmol/min/mg enzyme for N-valyl-L-asparagine2 Publications

    Vmax=92 µmol/min/mg enzyme for N-methionyl-L-asparagine2 Publications

    Vmax=8 µmol/min/mg enzyme for N-glycyl-D-asparagine2 Publications

    pH dependencei

    Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei43 – 431O-isoaspartyl threonine intermediatePROSITE-ProRule annotation
    Binding sitei89 – 891SubstrateBy similarity

    GO - Molecular functioni

    1. asparaginase activity Source: SGD

    GO - Biological processi

    1. asparagine catabolic process Source: SGD
    2. cellular response to nitrogen starvation Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciYEAST:YLR160C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-asparaginase 2-4 (EC:3.5.1.1)
    Alternative name(s):
    L-asparaginase II
    L-asparagine amidohydrolase II
    Short name:
    ASP II
    Gene namesi
    Name:ASP3-4
    Ordered Locus Names:YLR160C
    ORF Names:L9632.9
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR160c.
    SGDiS000004150. ASP3-4.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall-bounded periplasmic space Source: SGD
    2. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 362337L-asparaginase 2-4PRO_0000410443Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi31426. 1 interaction.
    31428. 15 interactions.
    31431. 22 interactions.
    31433. 17 interactions.
    IntActiP0CX79. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP0CX79.
    SMRiP0CX79. Positions 32-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1232Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the asparaginase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK01424.
    OrthoDBiEOG75TMN3.

    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.

    P0CX79-1 [UniParc]FASTAAdd to Basket

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    MRSLNTLLLS LFVAMSSGAP LLKIREEKNS SLPSIKIFGT GGTIASKGST    50
    SATTAGYSVG LTVNDLIEAV PSLAEKANLD YLQVSNVGSN SLNYTHLIPL 100
    YHGISEALAS DDYAGAVVTH GTDTMEETAF FLDLTINSEK PVCIAGAMRP 150
    ATATSADGPM NLYQAVSIAA SEKSLGRGTM ITLNDRIASG FWTTKMNANS 200
    LDTFRADEQG YLGYFSNDDV EFYYPPVKPN GWQFFDISNL TDPSEIPEVI 250
    ILYSYQGLNP ELIVKAVKDL GAKGIVLAGS GAGSWTATGS IVNEQLYEEY 300
    GIPIVHSRRT ADGTVPPDDA PEYAIGSGYL NPQKSRILLQ LCLYSGYGMD 350
    QIRSVFSGVY GG 362
    Length:362
    Mass (Da):38,687
    Last modified:June 28, 2011 - v1
    Checksum:i1DE5DC8692BF0461
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 5530Missing.1 Publication
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51921 Genomic DNA. Translation: AAB67484.1.
    BK006945 Genomic DNA. Translation: DAA09481.1.
    PIRiS68471.
    RefSeqiNP_013256.1. NM_001182042.1.
    NP_013258.1. NM_001182044.1.
    NP_013259.1. NM_001182045.1.
    NP_013261.1. NM_001182047.1.

    Genome annotation databases

    EnsemblFungiiYLR155C; YLR155C; YLR155C.
    YLR157C; YLR157C; YLR157C.
    YLR158C; YLR158C; YLR158C.
    YLR160C; YLR160C; YLR160C.
    GeneIDi850850.
    850852.
    850855.
    850857.
    KEGGisce:YLR155C.
    sce:YLR157C.
    sce:YLR158C.
    sce:YLR160C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51921 Genomic DNA. Translation: AAB67484.1 .
    BK006945 Genomic DNA. Translation: DAA09481.1 .
    PIRi S68471.
    RefSeqi NP_013256.1. NM_001182042.1.
    NP_013258.1. NM_001182044.1.
    NP_013259.1. NM_001182045.1.
    NP_013261.1. NM_001182047.1.

    3D structure databases

    ProteinModelPortali P0CX79.
    SMRi P0CX79. Positions 32-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31426. 1 interaction.
    31428. 15 interactions.
    31431. 22 interactions.
    31433. 17 interactions.
    IntActi P0CX79. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR155C ; YLR155C ; YLR155C .
    YLR157C ; YLR157C ; YLR157C .
    YLR158C ; YLR158C ; YLR158C .
    YLR160C ; YLR160C ; YLR160C .
    GeneIDi 850850.
    850852.
    850855.
    850857.
    KEGGi sce:YLR155C.
    sce:YLR157C.
    sce:YLR158C.
    sce:YLR160C.

    Organism-specific databases

    CYGDi YLR160c.
    SGDi S000004150. ASP3-4.

    Phylogenomic databases

    KOi K01424.
    OrthoDBi EOG75TMN3.

    Enzyme and pathway databases

    BioCyci YEAST:YLR160C-MONOMER.

    Miscellaneous databases

    NextBioi 967149.

    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. "Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene."
      Kim K.-W., Kamerud J.Q., Livingston D.M., Roon R.J.
      J. Biol. Chem. 263:11948-11953(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41 AND 56-71, VARIANT 26-GLU--ALA-55 DEL.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Characterization of two forms of asparaginase in Saccharomyces cerevisiae."
      Dunlop P.C., Meyer G.M., Ban D., Roon R.J.
      J. Biol. Chem. 253:1297-1304(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Nitrogen catabolite repression of asparaginase II in Saccharomyces cerevisiae."
      Dunlop P.C., Meyer G.M., Roon R.J.
      J. Bacteriol. 143:422-426(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. "Reactions of asparaginase II of Saccharomyces cerevisiae. A mechanistic analysis of hydrolysis and hydroxylaminolysis."
      Dunlop P.C., Meyer G.M., Roon R.J.
      J. Biol. Chem. 255:1542-1546(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiASP24_YEAST
    AccessioniPrimary (citable) accession number: P0CX79
    Secondary accession number(s): D6VYF3
    , P11163, Q12268, Q6Q5K8, Q6Q5K9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 24 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
    There are 4 copies for L-asparaginase 2 in yeast. The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in tandem repeats located near a ribosomal DNA cluster.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3