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O31465

- GLSA1_BACSU

UniProt

O31465 - GLSA1_BACSU

Protein

Glutaminase 1

Gene

glsA1

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 101 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-glutamine + H2O = L-glutamate + NH3.1 Publication

    Kineticsi

    1. KM=27.6 mM for glutamine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741Substrate
    Binding sitei126 – 1261Substrate
    Binding sitei170 – 1701Substrate
    Binding sitei177 – 1771Substrate
    Binding sitei201 – 2011Substrate
    Binding sitei253 – 2531Substrate
    Binding sitei271 – 2711Substrate; via amide nitrogen

    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:BSU02430-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaminase 1 (EC:3.5.1.2)
    Gene namesi
    Name:glsA1
    Synonyms:glsA, ybgJ
    Ordered Locus Names:BSU02430
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU02430. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 327327Glutaminase 1PRO_0000110594Add
    BLAST

    Proteomic databases

    PaxDbiO31465.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU02430.

    Structurei

    Secondary structure

    1
    327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2512
    Helixi26 – 316
    Helixi39 – 424
    Beta strandi50 – 545
    Beta strandi60 – 656
    Helixi73 – 753
    Helixi76 – 8813
    Helixi90 – 945
    Helixi110 – 1145
    Beta strandi123 – 1253
    Helixi126 – 13510
    Beta strandi136 – 1405
    Helixi141 – 15616
    Helixi164 – 17310
    Helixi175 – 18612
    Helixi194 – 20512
    Beta strandi207 – 2093
    Helixi211 – 22212
    Turni223 – 2253
    Turni228 – 2314
    Helixi237 – 25014
    Helixi253 – 2553
    Helixi256 – 2627
    Beta strandi267 – 2693
    Beta strandi273 – 2797
    Turni281 – 2844
    Turni288 – 2914
    Beta strandi293 – 2986
    Beta strandi306 – 3083
    Helixi309 – 32214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MKIX-ray2.00A/B1-327[»]
    2OSUX-ray2.29A/B1-327[»]
    3AGFX-ray2.60A/B1-327[»]
    3BRMX-ray2.29A/B1-327[»]
    ProteinModelPortaliO31465.
    SMRiO31465. Positions 1-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO31465.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutaminase family.Curated

    Phylogenomic databases

    eggNOGiCOG2066.
    HOGENOMiHOG000216890.
    KOiK01425.
    OMAiSANYIPA.
    OrthoDBiEOG6N94BK.
    PhylomeDBiO31465.

    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.

    O31465-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG    50
    ICVLEPDGTM IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE 100
    PTGDAFNSII RLEINKPGKP FNPMINAGAL TIASILPGES AYEKLEFLYS 150
    VMETLIGKRP RIHEEVFRSE WETAHRNRAL AYYLKETNFL EAEVEETLEV 200
    YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA KLAKALMLTC 250
    GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP 300
    AIDEYGNSLT GGMLLKHMAQ EWELSIF 327
    Length:327
    Mass (Da):36,187
    Last modified:January 1, 1998 - v1
    Checksum:iBE3A1C2366460287
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006424 Genomic DNA. Translation: BAA33141.1.
    AL009126 Genomic DNA. Translation: CAB12037.1.
    PIRiD69751.
    RefSeqiNP_388125.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12037; CAB12037; BSU02430.
    GeneIDi938416.
    KEGGibsu:BSU02430.
    PATRICi18972037. VBIBacSub10457_0247.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006424 Genomic DNA. Translation: BAA33141.1 .
    AL009126 Genomic DNA. Translation: CAB12037.1 .
    PIRi D69751.
    RefSeqi NP_388125.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MKI X-ray 2.00 A/B 1-327 [» ]
    2OSU X-ray 2.29 A/B 1-327 [» ]
    3AGF X-ray 2.60 A/B 1-327 [» ]
    3BRM X-ray 2.29 A/B 1-327 [» ]
    ProteinModelPortali O31465.
    SMRi O31465. Positions 1-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU02430.

    Proteomic databases

    PaxDbi O31465.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12037 ; CAB12037 ; BSU02430 .
    GeneIDi 938416.
    KEGGi bsu:BSU02430.
    PATRICi 18972037. VBIBacSub10457_0247.

    Organism-specific databases

    GenoListi BSU02430. [Micado ]

    Phylogenomic databases

    eggNOGi COG2066.
    HOGENOMi HOG000216890.
    KOi K01425.
    OMAi SANYIPA.
    OrthoDBi EOG6N94BK.
    PhylomeDBi O31465.

    Enzyme and pathway databases

    BioCyci BSUB:BSU02430-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O31465.
    PROi O31465.

    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. "Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome."
      Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.
      Submitted (JUL-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. "Enhancement of glutamine utilization in Bacillus subtilis through the GlnK-GlnL two-component regulatory system."
      Satomura T., Shimura D., Asai K., Sadaie Y., Hirooka K., Fujita Y.
      J. Bacteriol. 187:4813-4821(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GENE NAME.
      Strain: 168.
    4. "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: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR 5-OXO-L-NORLEUCINE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiGLSA1_BACSU
    AccessioniPrimary (citable) accession number: O31465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 101 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3