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P54420

- ASNB_BACSU

UniProt

P54420 - ASNB_BACSU

Protein

Asparagine synthetase [glutamine-hydrolyzing] 1

Gene

asnB

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 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Main asparagine synthetase in vegetative cells.

    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
    Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Sitei363 – 3631Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi361 – 3622ATPBy 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:BSU30540-MONOMER.
    UniPathwayiUPA00134; UER00195.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 1 (EC:6.3.5.4)
    Gene namesi
    Name:asnB
    Synonyms:asn
    Ordered Locus Names:BSU30540
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU30540. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 632631Asparagine synthetase [glutamine-hydrolyzing] 1PRO_0000056932Add
    BLAST

    Proteomic databases

    PaxDbiP54420.

    Interactioni

    Protein-protein interaction databases

    IntActiP54420. 3 interactions.
    MINTiMINT-8366280.
    STRINGi224308.BSU30540.

    Structurei

    3D structure databases

    ProteinModelPortaliP54420.
    SMRiP54420. Positions 2-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 214213Glutamine 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.
    HOGENOMiHOG000027495.
    KOiK01953.
    OMAiYFASERK.
    OrthoDBiEOG6P8TM1.
    PhylomeDBiP54420.

    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.

    P54420-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGFVGVFNK HPLAQTADQE ELIKQMNQMI VHRGPDSDGY FHDEHVGFGF    50
    RRLSIIDVEN GGQPLSYEDE TYWIIFNGEI YNYIELREEL EAKGYTFNTD 100
    SDTEVLLATY RHYKEEAASK LRGMFAFLIW NKNDHVLYGA RDPFGIKPLY 150
    YTTINDQVYF ASERKSLMVA QNDIEIDKEA LQQYMSFQFV PEPSTLDAHV 200
    KKVEPGSQFT IRPDGDITFK TYFKANFKPV QTEEDKLVKE VRDAIYDSVN 250
    VHMRSDVPVG SFLSGGIDSS FIVSVAKEFH PSLKTFSVGF EQQGFSEVDV 300
    AKETAAALGI ENISKVISPE EYMNELPKIV WHFDDPLADP AAIPLYFVAK 350
    EAKKHVTVAL SGEGADELFG GYNIYREPLS LKPFERIPSG LKKMLLHVAA 400
    VMPEGMRGKS LLERGCTPLQ DRYIGNAKIF EESVKKQLLK HYNPNLSYRD 450
    VTKTYFTESS SYSDINKMQY VDIHTWMRGD ILLKADKMTM ANSLELRVPF 500
    LDKVVFDVAS KIPDELKTKN GTTKYLLRKA AEGIVPEHVL NRKKLGFPVP 550
    IRHWLKNEMN EWVRNIIQES QTDAYIHKDY VLQLLEDHCA DKADNSRKIW 600
    TVLIFMIWHS INIEKRYMPE ELSHQPKEVI FV 632
    Length:632
    Mass (Da):72,666
    Last modified:May 30, 2000 - v2
    Checksum:i155F11E6988901EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 813EIY → VNL in AAB17067. (PubMed:9384377)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF008220 Genomic DNA. Translation: AAC00243.1.
    AL009126 Genomic DNA. Translation: CAB15032.1.
    U52812 Genomic DNA. Translation: AAB17067.1.
    PIRiH69590.
    RefSeqiNP_390932.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15032; CAB15032; BSU30540.
    GeneIDi937236.
    KEGGibsu:BSU30540.
    PATRICi18978012. VBIBacSub10457_3194.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF008220 Genomic DNA. Translation: AAC00243.1 .
    AL009126 Genomic DNA. Translation: CAB15032.1 .
    U52812 Genomic DNA. Translation: AAB17067.1 .
    PIRi H69590.
    RefSeqi NP_390932.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P54420.
    SMRi P54420. Positions 2-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P54420. 3 interactions.
    MINTi MINT-8366280.
    STRINGi 224308.BSU30540.

    Proteomic databases

    PaxDbi P54420.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15032 ; CAB15032 ; BSU30540 .
    GeneIDi 937236.
    KEGGi bsu:BSU30540.
    PATRICi 18978012. VBIBacSub10457_3194.

    Organism-specific databases

    GenoListi BSU30540. [Micado ]

    Phylogenomic databases

    eggNOGi COG0367.
    HOGENOMi HOG000027495.
    KOi K01953.
    OMAi YFASERK.
    OrthoDBi EOG6P8TM1.
    PhylomeDBi P54420.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .
    BioCyci BSUB:BSU30540-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. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
      Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
      Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    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. "Cloning and characterization of the metE gene encoding S-adenosylmethionine synthetase from Bacillus subtilis."
      Yocum R., Perkins J.B., Howitt C.L., Pero J.
      J. Bacteriol. 178:4604-4610(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
      Strain: 168 / PY79.
    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 nameiASNB_BACSU
    AccessioniPrimary (citable) accession number: P54420
    Secondary accession number(s): O34902
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 108 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