ID   GLSA_BACMK              Reviewed;         309 AA.
AC   A9VSP6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 86.
DE   RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313};
GN   OrderedLocusNames=BcerKBAB4_0416;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamine + H2O = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00313};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00313}.
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DR   EMBL; CP000903; ABY41682.1; -; Genomic_DNA.
DR   RefSeq; WP_002029606.1; NC_010184.1.
DR   AlphaFoldDB; A9VSP6; -.
DR   SMR; A9VSP6; -.
DR   KEGG; bwe:BcerKBAB4_0416; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_0_9; -.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006543; P:L-glutamine catabolic process; IEA:TreeGrafter.
DR   FunFam; 1.10.1500.10:FF:000001; Glutaminase; 1.
DR   FunFam; 3.40.710.10:FF:000005; Glutaminase; 1.
DR   Gene3D; 1.10.1500.10; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..309
FT                   /note="Glutaminase"
FT                   /id="PRO_1000115692"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   309 AA;  34003 MW;  050BEE3C71F6E27D CRC64;
     MQCIETNNLQ QLLEQVKPYT KKGKLATYIP ELGNANPNDL GIAIFHKETE YIHAGNSQTL
     FTLQSISKVI TLALALLDRG EEYVFSKVGM EPTGDPFNSI IKLETTSSSK PLNPMINAGA
     LAITSMLAGN DNEEKMERIL QFVRDITDNP TISYSSKVAT SELETAYLNR SLCYYMKQNG
     IIDNDIEELM DLYTRQCAIE VNCIDLARIG LIFAMDGYDP YKKKQIIPKH ITKICKTFMV
     TCGMYNESGE FAIRVGIPAK SGVAGGIFGC VKGEMGIGIF GPALDANGNS IAGFKILELL
     SAQEGWSMF
//