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O07637

- GLSA2_BACSU

UniProt

O07637 - GLSA2_BACSU

Protein

Glutaminase 2

Gene

glsA2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-glutamine + H2O = L-glutamate + NH3.1 PublicationUniRule annotation

    Kineticsi

    1. KM=7.6 mM for glutamine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651SubstrateUniRule annotation
    Binding sitei117 – 1171SubstrateUniRule annotation
    Binding sitei162 – 1621SubstrateUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Binding sitei193 – 1931SubstrateUniRule annotation
    Binding sitei245 – 2451SubstrateUniRule annotation
    Binding sitei263 – 2631Substrate; via amide nitrogenUniRule annotation

    GO - Molecular functioni

    1. glutaminase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. glutamine metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciBSUB:BSU14830-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaminase 2UniRule annotation (EC:3.5.1.2UniRule annotation)
    Gene namesi
    Name:glsA2UniRule annotation
    Synonyms:ylaM
    Ordered Locus Names:BSU14830
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU14830. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Glutaminase 2PRO_0000110595Add
    BLAST

    Proteomic databases

    PaxDbiO07637.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi224308.BSU14830.

    Structurei

    3D structure databases

    ProteinModelPortaliO07637.
    SMRiO07637. Positions 4-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutaminase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2066.
    HOGENOMiHOG000216890.
    KOiK01425.
    OMAiQRARRIN.
    OrthoDBiEOG6N94BK.
    PhylomeDBiO07637.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    HAMAPiMF_00313. Glutaminase.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view]
    PANTHERiPTHR12544. PTHR12544. 1 hit.
    PfamiPF04960. Glutaminase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    TIGRFAMsiTIGR03814. Gln_ase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O07637-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVCQHNDELE ALVKKAKKVT DKGEVASYIP ALAKADKHDL SVAIYYSNNV    50
    CLSAGDVEKT FTLQSISKVL SLALVLMEYG KDKVFSYVGQ EPTGDPFNSI 100
    IKLETVNPSK PLNPMINAGA LVVTSLIRGR TVKERLDYLL SFIRRLTNNQ 150
    EITYCREVAE SEYSTSMINR AMCYYMKQYG IFEDDVEAVM DLYTKQCAIE 200
    MNSLDLAKIG SVFALNGRHP ETGEQVISKD VARICKTFMV TCGMYNASGE 250
    FAIKVGIPAK SGVSGGIMGI SPYDFGIGIF GPALDEKGNS IAGVKLLEIM 300
    SEMYRLSIF 309
    Length:309
    Mass (Da):34,012
    Last modified:July 1, 1997 - v1
    Checksum:iE1DFEF1A0723C1A5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97025 Genomic DNA. Translation: CAB09718.1.
    AL009126 Genomic DNA. Translation: CAB13356.1.
    PIRiC69873.
    RefSeqiNP_389366.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13356; CAB13356; BSU14830.
    GeneIDi939852.
    KEGGibsu:BSU14830.
    PATRICi18974763. VBIBacSub10457_1573.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z97025 Genomic DNA. Translation: CAB09718.1 .
    AL009126 Genomic DNA. Translation: CAB13356.1 .
    PIRi C69873.
    RefSeqi NP_389366.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O07637.
    SMRi O07637. Positions 4-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU14830.

    Proteomic databases

    PaxDbi O07637.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13356 ; CAB13356 ; BSU14830 .
    GeneIDi 939852.
    KEGGi bsu:BSU14830.
    PATRICi 18974763. VBIBacSub10457_1573.

    Organism-specific databases

    GenoListi BSU14830. [Micado ]

    Phylogenomic databases

    eggNOGi COG2066.
    HOGENOMi HOG000216890.
    KOi K01425.
    OMAi QRARRIN.
    OrthoDBi EOG6N94BK.
    PhylomeDBi O07637.

    Enzyme and pathway databases

    BioCyci BSUB:BSU14830-MONOMER.

    Miscellaneous databases

    PROi O07637.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    HAMAPi MF_00313. Glutaminase.
    InterProi IPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view ]
    PANTHERi PTHR12544. PTHR12544. 1 hit.
    Pfami PF04960. Glutaminase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56601. SSF56601. 1 hit.
    TIGRFAMsi TIGR03814. Gln_ase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Bacillus subtilis chromosomal region downstream nprE."
      Purnelle B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      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. "Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis."
      Brown G., Singer A., Proudfoot M., Skarina T., Kim Y., Chang C., Dementieva I., Kuznetsova E., Gonzalez C.F., Joachimiak A., Savchenko A., Yakunin A.F.
      Biochemistry 47:5724-5735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiGLSA2_BACSU
    AccessioniPrimary (citable) accession number: O07637
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 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