ID B7IMN2_BACC2 Unreviewed; 326 AA.
AC B7IMN2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Glutaminase {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
GN Name=glsA2 {ECO:0000313|EMBL:ACK97782.1};
GN Synonyms=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN OrderedLocusNames=BCG9842_B2097 {ECO:0000313|EMBL:ACK97782.1};
OS Bacillus cereus (strain G9842).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK97782.1, ECO:0000313|Proteomes:UP000006744};
RN [1] {ECO:0000313|EMBL:ACK97782.1, ECO:0000313|Proteomes:UP000006744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842 {ECO:0000313|EMBL:ACK97782.1,
RC ECO:0000313|Proteomes:UP000006744};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC Rule:MF_00313};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076, ECO:0000256|HAMAP-Rule:MF_00313}.
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DR EMBL; CP001186; ACK97782.1; -; Genomic_DNA.
DR RefSeq; WP_000588648.1; NC_011772.1.
DR AlphaFoldDB; B7IMN2; -.
DR SMR; B7IMN2; -.
DR KEGG; bcg:BCG9842_B2097; -.
DR HOGENOM; CLU_027932_1_0_9; -.
DR Proteomes; UP000006744; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
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:SF32; GLUTAMINASE 1; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00313}.
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 326 AA; 35856 MW; 24E302EF2E8F56A1 CRC64;
MIKDSSVQVE GQEKVCLDQW VAHYRAYAAK GRSASYIPAL GEINVSQLGI CIVKPDGTMI
KSGDWEIPFT LQSISKVIGF IAACLSRGIS YVLERVDVEP TGDAFNSIIR LEIHKPGKPF
NPMINAGAIT IASLLPGTSV QEKLESLYVL IEKMIEKRPA INEIVFQSEW ETAHRNRALA
YYLKENGFLE SDVEETLEVY LKQCSIEINT EDIALIGLIL AHDGYHPIRK EQVLPKEVAR
LTKALMLTCG MYNASGKFAA FIGLPAKSGV SGGIMTLVPS KSRKDLSFQD GCGIGIYGPA
IDEYGNSLPG IMLLEHIAKE WDLSIF
//
