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Protein

Glutaminase 1

Gene

glsA1

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciBSUB:BSU02430-MONOMER.
    BRENDAi3.5.1.2. 658.
    4.3.3.6. 658.

    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 Componenti: 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.Bsubs1_010100001348.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    InParanoidiO31465.
    KOiK01425.
    OMAiPMNPMVN.
    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

            10         20         30         40         50
    MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG
    60 70 80 90 100
    ICVLEPDGTM IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE
    110 120 130 140 150
    PTGDAFNSII RLEINKPGKP FNPMINAGAL TIASILPGES AYEKLEFLYS
    160 170 180 190 200
    VMETLIGKRP RIHEEVFRSE WETAHRNRAL AYYLKETNFL EAEVEETLEV
    210 220 230 240 250
    YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA KLAKALMLTC
    260 270 280 290 300
    GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP
    310 320
    AIDEYGNSLT GGMLLKHMAQ EWELSIF
    Length:327
    Mass (Da):36,187
    Last modified:January 1, 1998 - v1
    Checksum:iBE3A1C2366460287
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB006424 Genomic DNA. Translation: BAA33141.1.
    AL009126 Genomic DNA. Translation: CAB12037.1.
    PIRiD69751.
    RefSeqiNP_388125.1. NC_000964.3.
    WP_003234829.1. NZ_JNCM01000030.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB006424 Genomic DNA. Translation: BAA33141.1.
    AL009126 Genomic DNA. Translation: CAB12037.1.
    PIRiD69751.
    RefSeqiNP_388125.1. NC_000964.3.
    WP_003234829.1. NZ_JNCM01000030.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100001348.

    Proteomic databases

    PaxDbiO31465.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GenoListiBSU02430. [Micado]

    Phylogenomic databases

    eggNOGiCOG2066.
    HOGENOMiHOG000216890.
    InParanoidiO31465.
    KOiK01425.
    OMAiPMNPMVN.
    OrthoDBiEOG6N94BK.
    PhylomeDBiO31465.

    Enzyme and pathway databases

    BioCyciBSUB:BSU02430-MONOMER.
    BRENDAi3.5.1.2. 658.
    4.3.3.6. 658.

    Miscellaneous databases

    EvolutionaryTraceiO31465.
    PROiO31465.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 108 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.