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P42113

- ASNH_BACSU

UniProt

P42113 - ASNH_BACSU

Protein

Asparagine synthetase [glutamine-hydrolyzing] 2

Gene

asnH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      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 sitei100 – 1001GlutamineBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi395 – 3962ATPBy 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

    BioCyciBSUB:BSU39920-MONOMER.
    UniPathwayiUPA00134; UER00195.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 2 (EC:6.3.5.4)
    Gene namesi
    Name:asnH
    Synonyms:yxaN
    Ordered Locus Names:BSU39920
    ORF Names:S14NR, VE7AR
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU39920. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 747746Asparagine synthetase [glutamine-hydrolyzing] 2PRO_0000056933Add
    BLAST

    Proteomic databases

    PaxDbiP42113.
    PRIDEiP42113.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU39920.

    Structurei

    3D structure databases

    ProteinModelPortaliP42113.
    SMRiP42113. Positions 2-542.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 218217Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 565Glutamine bindingBy similarity
    Regioni77 – 793Glutamine bindingBy similarity

    Sequence similaritiesi

    Belongs to the asparagine synthetase family.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0367.
    HOGENOMiHOG000155832.
    KOiK01953.
    OrthoDBiEOG6P8TM1.
    PhylomeDBiP42113.

    Family and domain databases

    Gene3Di3.40.50.620. 2 hits.
    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.

    P42113-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGLAGIINL AAPRSQECTF HILKGMADAI SYRGPDDEQY HIDSKVGFAF    50
    RRLSILDLVN GQQPFLNEDG SIVVMVNGEI YNYKELKASL HNHMFKTTSD 100
    CEVIVHLYEE KGIGFVDDII GMFSIAIWDK NKNKVFLVRD RFGIKPLFYT 150
    ELKHELIFAS EIKSLFSHPH CPRQFNWKEA LSDIWLSGEA ASNHKETTSF 200
    FVNIQNLDAG HYLEINLTTN ERKTASYWSL QDILLRQGYR ENLHPDDLIE 250
    GYRELLADSV HRCLQSDVEV GLFLSGGIDS AAVAHFAAEK QDLHTFTVLS 300
    QSTFTNEDAK YAHWLAKDLH LPNHQVLYQL GNDELLQPES YKHLLWICET 350
    PFCGPEQLYK FHLHKYAKAI RPNLKVMLTG QGSDEFNGGY STTLSPAENP 400
    SWEGFIESVN TMEMNRLHRL QGNIFRVWEE HFGLSPINLS YLKSNDSSQA 450
    DPWQSYVLTK YRDLQMYNCW HEDRIAAANH IENRVPFLDH RLVEWVCGIP 500
    DGLRKDLLWD KSVLRKSLTN ELHTSYTHRP KVPFFYGKDV RYTHKMMFHL 550
    LKKNNYQLIE EAFSHSDASS IIQVEHIHAI MTYLEDDPEF TNFEFLLRLV 600
    NMGLLSKMTK ETPSVQLDIT SHLESITIKD WHSQEGDIAS RLNISANKCE 650
    GQDILALNPG VTLLRPESDS EHCIYIAEEG FIQFIVSEED VGAWLHILCD 700
    INGKDTLHTI LDRHGVSLEE VAKYIQEAIE HNIILIKQKN LPEGAYR 747
    Length:747
    Mass (Da):85,932
    Last modified:July 28, 2009 - v2
    Checksum:iE1447AC0B72922CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti185 – 1851W → C in BAA21593. (PubMed:7584049)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB005554 Genomic DNA. Translation: BAA21593.1.
    AL009126 Genomic DNA. Translation: CAB16028.2.
    PIRiA69591.
    RefSeqiNP_391871.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB16028; CAB16028; BSU39920.
    GeneIDi937677.
    KEGGibsu:BSU39920.
    PATRICi18980052. VBIBacSub10457_4188.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB005554 Genomic DNA. Translation: BAA21593.1 .
    AL009126 Genomic DNA. Translation: CAB16028.2 .
    PIRi A69591.
    RefSeqi NP_391871.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P42113.
    SMRi P42113. Positions 2-542.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU39920.

    Proteomic databases

    PaxDbi P42113.
    PRIDEi P42113.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB16028 ; CAB16028 ; BSU39920 .
    GeneIDi 937677.
    KEGGi bsu:BSU39920.
    PATRICi 18980052. VBIBacSub10457_4188.

    Organism-specific databases

    GenoListi BSU39920. [Micado ]

    Phylogenomic databases

    eggNOGi COG0367.
    HOGENOMi HOG000155832.
    KOi K01953.
    OrthoDBi EOG6P8TM1.
    PhylomeDBi P42113.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .
    BioCyci BSUB:BSU39920-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.620. 2 hits.
    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. "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons."
      Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.
      DNA Res. 2:61-69(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / BGSC1A1.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 185.
    4. "Three asparagine synthetase genes of Bacillus subtilis."
      Yoshida K., Fujita Y., Ehrlich S.D.
      J. Bacteriol. 181:6081-6091(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiASNH_BACSU
    AccessioniPrimary (citable) accession number: P42113
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3