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Database: UniProt
Entry: R8GZZ5_BACCE
LinkDB: R8GZZ5_BACCE
Original site: R8GZZ5_BACCE 
ID   R8GZZ5_BACCE            Unreviewed;       309 AA.
AC   R8GZZ5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN   ORFNames=IIC_05841 {ECO:0000313|EMBL:EOO66168.1};
OS   Bacillus cereus VD021.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053224 {ECO:0000313|EMBL:EOO66168.1, ECO:0000313|Proteomes:UP000014040};
RN   [1] {ECO:0000313|EMBL:EOO66168.1, ECO:0000313|Proteomes:UP000014040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VD021 {ECO:0000313|EMBL:EOO66168.1,
RC   ECO:0000313|Proteomes:UP000014040};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus VD021.";
RL   Submitted (DEC-2012) 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|ARBA:ARBA00011881,
CC       ECO:0000256|HAMAP-Rule:MF_00313}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076, ECO:0000256|HAMAP-Rule:MF_00313}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOO66168.1}.
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DR   EMBL; AHES01000077; EOO66168.1; -; Genomic_DNA.
DR   RefSeq; WP_002029606.1; NZ_KB976285.1.
DR   AlphaFoldDB; R8GZZ5; -.
DR   SMR; R8GZZ5; -.
DR   PATRIC; fig|1053224.3.peg.5875; -.
DR   HOGENOM; CLU_027932_1_0_9; -.
DR   Proteomes; UP000014040; Unassembled WGS sequence.
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:SF29; GLUTAMINASE; 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         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         162
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         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|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
//
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