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O30509

- GATB_BACSU

UniProt

O30509 - GATB_BACSU

Protein

Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B

Gene

gatB

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 95 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).

    Catalytic activityi

    ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
    ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro

    GO - Biological processi

    1. translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU06690-MONOMER.
    MetaCyc:MONOMER-13956.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (EC:6.3.5.-)
    Short name:
    Asp/Glu-ADT subunit B
    Gene namesi
    Name:gatB
    Synonyms:yerN
    Ordered Locus Names:BSU06690
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU06690. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 476476Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit BPRO_0000148762Add
    BLAST

    Proteomic databases

    PaxDbiO30509.

    Interactioni

    Subunit structurei

    Heterotrimer of A, B and C subunits.

    Protein-protein interaction databases

    IntActiO30509. 1 interaction.
    MINTiMINT-8366537.
    STRINGi224308.BSU06690.

    Structurei

    3D structure databases

    ProteinModelPortaliO30509.
    SMRiO30509. Positions 1-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GatB/GatE family. GatB subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0064.
    HOGENOMiHOG000223742.
    KOiK02434.
    OrthoDBiEOG6RJV5B.

    Family and domain databases

    HAMAPiMF_00121. GatB.
    InterProiIPR004413. Apn/Gln-ADT_bsu.
    IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
    IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
    IPR018027. Asn/Gln_amidotransferase.
    IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
    IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
    [Graphical view]
    PANTHERiPTHR11659. PTHR11659. 1 hit.
    PfamiPF02934. GatB_N. 1 hit.
    PF02637. GatB_Yqey. 1 hit.
    [Graphical view]
    SMARTiSM00845. GatB_Yqey. 1 hit.
    [Graphical view]
    SUPFAMiSSF89095. SSF89095. 1 hit.
    TIGRFAMsiTIGR00133. gatB. 1 hit.
    PROSITEiPS01234. GATB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O30509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNFETVIGLE VHVELKTKSK IFSSSPTPFG AEANTQTSVI DLGYPGVLPV    50
    LNKEAVEFAM KAAMALNCEI ATDTKFDRKN YFYPDNPKAY QISQFDKPIG 100
    ENGWIEIEVG GKTKRIGITR LHLEEDAGKL THTGDGYSLV DFNRQGTPLV 150
    EIVSEPDIRT PEEAYAYLEK LKSIIQYTGV SDCKMEEGSL RCDANISLRP 200
    IGQEEFGTKT ELKNLNSFAF VQKGLEHEEK RQEQVLLSGF FIQQETRRYD 250
    EATKKTILMR VKEGSDDYRY FPEPDLVELY IDDEWKERVK ASIPELPDER 300
    RKRYIEELGF AAYDAMVLTL TKEMADFFEE TVQKGAEAKQ ASNWLMGEVS 350
    AYLNAEQKEL ADVALTPEGL AGMIKLIEKG TISSKIAKKV FKELIEKGGD 400
    AEKIVKEKGL VQISDEGVLL KLVTEALDNN PQSIEDFKNG KDRAIGFLVG 450
    QIMKASKGQA NPPMVNKILL EEIKKR 476
    Length:476
    Mass (Da):53,553
    Last modified:May 30, 2000 - v2
    Checksum:i095B056BF4B44676
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 282TP → PN in AAB87634. 1 PublicationCurated
    Sequence conflicti43 – 431G → A in AAB87634. 1 PublicationCurated
    Sequence conflicti240 – 2412FF → GV in CAB12489. (PubMed:9384377)Curated
    Sequence conflicti310 – 3112FA → LP in CAB12489. (PubMed:9384377)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49788 Genomic DNA. Translation: AAB87634.1.
    AF008553 Genomic DNA. Translation: AAB83965.1.
    AL009126 Genomic DNA. Translation: CAB12489.2.
    PIRiT51583.
    RefSeqiNP_388551.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12489; CAB12489; BSU06690.
    GeneIDi936057.
    KEGGibsu:BSU06690.
    PATRICi18972984. VBIBacSub10457_0706.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49788 Genomic DNA. Translation: AAB87634.1 .
    AF008553 Genomic DNA. Translation: AAB83965.1 .
    AL009126 Genomic DNA. Translation: CAB12489.2 .
    PIRi T51583.
    RefSeqi NP_388551.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali O30509.
    SMRi O30509. Positions 1-476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O30509. 1 interaction.
    MINTi MINT-8366537.
    STRINGi 224308.BSU06690.

    Proteomic databases

    PaxDbi O30509.

    Protocols and materials databases

    DNASUi 936057.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12489 ; CAB12489 ; BSU06690 .
    GeneIDi 936057.
    KEGGi bsu:BSU06690.
    PATRICi 18972984. VBIBacSub10457_0706.

    Organism-specific databases

    GenoListi BSU06690. [Micado ]

    Phylogenomic databases

    eggNOGi COG0064.
    HOGENOMi HOG000223742.
    KOi K02434.
    OrthoDBi EOG6RJV5B.

    Enzyme and pathway databases

    BioCyci BSUB:BSU06690-MONOMER.
    MetaCyc:MONOMER-13956.

    Family and domain databases

    HAMAPi MF_00121. GatB.
    InterProi IPR004413. Apn/Gln-ADT_bsu.
    IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
    IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
    IPR018027. Asn/Gln_amidotransferase.
    IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
    IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
    [Graphical view ]
    PANTHERi PTHR11659. PTHR11659. 1 hit.
    Pfami PF02934. GatB_N. 1 hit.
    PF02637. GatB_Yqey. 1 hit.
    [Graphical view ]
    SMARTi SM00845. GatB_Yqey. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89095. SSF89095. 1 hit.
    TIGRFAMsi TIGR00133. gatB. 1 hit.
    PROSITEi PS01234. GATB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation."
      Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W., Henkin T.M., Soell D.
      Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
      Strain: 168.
    2. Hong K.-W., Martins O.M., Kim S.-I., Soell D.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.

    Entry informationi

    Entry nameiGATB_BACSU
    AccessioniPrimary (citable) accession number: O30509
    Secondary accession number(s): O31499, O50554
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 95 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3