GLSA_BACMK
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 03-AUG-2022, entry version 73.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC 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=H2O + L-glutamine = 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 STRING; 315730.BcerKBAB4_0416; -.
DR EnsemblBacteria; ABY41682; ABY41682; BcerKBAB4_0416.
DR KEGG; bwe:BcerKBAB4_0416; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_9; -.
DR OMA; RPRNPFI; -.
DR Proteomes; UP000002154; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 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