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P17714

- ASNS_MESAU

UniProt

P17714 - ASNS_MESAU

Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene

ASNS

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21For GATase activityBy similarity
    Binding sitei97 – 971GlutamineBy similarity
    Binding sitei256 – 2561ATP; via carbonyl oxygenBy similarity
    Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Sitei365 – 3651Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi363 – 3642ATPBy similarity

    GO - Molecular functioni

    1. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB-KW
    2. L-asparagine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Asparagine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00134; UER00195.

    Protein family/group databases

    MEROPSiC44.974.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
    Alternative name(s):
    Glutamine-dependent asparagine synthetase
    Gene namesi
    Name:ASNS
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi414 – 4141L → F in ts11; temperature-sensitive. Blocked in the G1 phase of the cell cycle at the non-permissive temperature (39.5 degrees Celsius). Heat labile.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056911Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei385 – 3851N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Structurei

    3D structure databases

    ProteinModelPortaliP17714.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 191190Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 536324Asparagine synthetaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 535Glutamine bindingBy similarity
    Regioni75 – 773Glutamine bindingBy similarity

    Sequence similaritiesi

    Contains 1 asparagine synthetase domain.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    HOVERGENiHBG003103.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProiIPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17714-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL    50
    AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI 100
    ILHLYDKGGI EQTICMLDGV FAFILLDTAN KKVFLGRDTY GVRPLFKAMT 150
    EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF LPGHYEVLDL KPNGKVASVE 200
    MVKYHHCRDE PLHALYDSVE KLFPGFELET VKSNLRILFD NAVRKRLMTD 250
    RRIVCLLSGG LDSSLVASSL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR 300
    KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK 350
    YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF 400
    DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRVPK NGIEKHLLRE 450
    TFEDSNLLPK EILWRPKEAF SDGITSVKNS WFKILQDYVE HQVDDAMMAT 500
    AAQKFPFNTP KTKEGYFYRQ IFEHHYPGRA DWLTHYWMPK WINATDPSAR 550
    TLTHYKSAAK A 561
    Length:561
    Mass (Da):64,274
    Last modified:January 23, 2007 - v3
    Checksum:i69DF791ED0FA0EF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52130 mRNA. Translation: CAA36375.1.
    PIRiS12740. AJHYNG.
    RefSeqiNP_001268543.1. NM_001281614.1.

    Genome annotation databases

    GeneIDi101836926.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52130 mRNA. Translation: CAA36375.1 .
    PIRi S12740. AJHYNG.
    RefSeqi NP_001268543.1. NM_001281614.1.

    3D structure databases

    ProteinModelPortali P17714.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C44.974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101836926.

    Organism-specific databases

    CTDi 440.

    Phylogenomic databases

    HOVERGENi HBG003103.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProi IPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A mammalian temperature-sensitive mutation affecting G1 progression results from a single amino acid substitution in asparagine synthetase."
      Gong S.S., Basilico C.
      Nucleic Acids Res. 18:3509-3513(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTANTS TS11.
      Strain: Syrian.

    Entry informationi

    Entry nameiASNS_MESAU
    AccessioniPrimary (citable) accession number: P17714
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The temperature-sensitive mutation affecting G1 progression results from a single amino acid substitution.

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3