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O05272

- ASNO_BACSU

UniProt

O05272 - ASNO_BACSU

Protein

Asparagine synthetase [glutamine-hydrolyzing] 3

Gene

asnO

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (30 May 2000)
      Previous versions | rss
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    Functioni

    Asparagine synthetase involved in sporulation.

    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 sitei102 – 1021GlutamineBy similarity
    Sitei379 – 3791Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi377 – 3782ATPBy 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
    3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Asparagine biosynthesis, Sporulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU10790-MONOMER.
    UniPathwayiUPA00134; UER00195.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 3 (EC:6.3.5.4)
    Gene namesi
    Name:asnO
    Synonyms:yisO, yucB
    Ordered Locus Names:BSU10790
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU10790. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 614613Asparagine synthetase [glutamine-hydrolyzing] 3PRO_0000056934Add
    BLAST

    Proteomic databases

    PaxDbiO05272.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU10790.

    Structurei

    3D structure databases

    ProteinModelPortaliO05272.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 216215Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 545Glutamine 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.
    HOGENOMiHOG000027494.
    KOiK01953.
    OMAiFGQLMSG.
    OrthoDBiEOG6Q5NPQ.
    PhylomeDBiO05272.

    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.

    O05272-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGITGWVDF KKQLVQEKQT MDRMTDTLSK RGPDDSNVWG EHHVLFGHKR    50
    LAVVDIEGGR QPMACTYKGD TYTIIYNGEL YNTEDLRKEL RARGHQFERT 100
    SDTEVLLHSY IEWQEDCVDH LNGIFAFAVW DEKRNLLFAA RDRLGVKPFF 150
    YTKEGSSFLF GSEIKAILAH PDIKARVDRT GLSEIFGLGP SRTPGTGIFK 200
    GIKEIRPAHA LTFSKDGLNI WRYWNVESEK HTDSFDDTVA NVRSLFQDAV 250
    TRQLVSDVPV CTFLSGGLDS SAITAIAAGH FEKEGKAPLH TYSIDYEEND 300
    KYFQASAFQP NDDGPWIEKM TEAFGTTHHK CVISQKDLVD HLEEAVLVKD 350
    LPGMADVDSS LLWFCREIKK DFVVSLSGEC ADEIFGGYPW FHTADVESGF 400
    PWMRSTEERI KLLSDSWQKK LNLKEYVNAK YEETLAETPL LDGETGVDKA 450
    RRQLFYLNML WFMTNLLDRK DRMSMGASLE VRVPFADHRL VEYVWNIPWE 500
    MKMHDNREKG ILRKALEGIL PDDILYRKKS PYPKTHHPEY TKGVSEWLKT 550
    IRSQKDSVLH TLLDRKQLDQ LLETEGSSFK VPWFGQLMKG PQLIAHLAQI 600
    HTWFEAYRID IDER 614
    Length:614
    Mass (Da):70,714
    Last modified:May 30, 2000 - v3
    Checksum:iD621D9A4557A8AC1
    GO

    Sequence cautioni

    The sequence CAA70643.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z93940 Genomic DNA. Translation: CAB07965.1.
    Y09476 Genomic DNA. Translation: CAA70643.1. Different initiation.
    AL009126 Genomic DNA. Translation: CAB12919.2.
    PIRiF69837.
    RefSeqiNP_388960.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12919; CAB12919; BSU10790.
    GeneIDi939783.
    KEGGibsu:BSU10790.
    PATRICi18973862. VBIBacSub10457_1125.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z93940 Genomic DNA. Translation: CAB07965.1 .
    Y09476 Genomic DNA. Translation: CAA70643.1 . Different initiation.
    AL009126 Genomic DNA. Translation: CAB12919.2 .
    PIRi F69837.
    RefSeqi NP_388960.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali O05272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU10790.

    Proteomic databases

    PaxDbi O05272.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12919 ; CAB12919 ; BSU10790 .
    GeneIDi 939783.
    KEGGi bsu:BSU10790.
    PATRICi 18973862. VBIBacSub10457_1125.

    Organism-specific databases

    GenoListi BSU10790. [Micado ]

    Phylogenomic databases

    eggNOGi COG0367.
    HOGENOMi HOG000027494.
    KOi K01953.
    OMAi FGQLMSG.
    OrthoDBi EOG6Q5NPQ.
    PhylomeDBi O05272.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .
    BioCyci BSUB:BSU10790-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. "Bacillus subtilis genome project, DNA sequence from yucA to yucH."
      Oudega B., Koningstein G., Duesterhoeft A.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis."
      Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.
      Microbiology 143:3305-3308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "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.
    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 nameiASNO_BACSU
    AccessioniPrimary (citable) accession number: O05272
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 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