ID A0A1C3S8D0_9BACI Unreviewed; 327 AA.
AC A0A1C3S8D0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ECO:0000313|EMBL:SCA84104.1};
GN ORFNames=BGLY_0281 {ECO:0000313|EMBL:SCA84104.1}, EQZ20_01570
GN {ECO:0000313|EMBL:QAT63762.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:SCA84104.1, ECO:0000313|Proteomes:UP000093092};
RN [1] {ECO:0000313|Proteomes:UP000093092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SCA84104.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BGLY {ECO:0000313|EMBL:SCA84104.1};
RA Schneider J.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QAT63762.1, ECO:0000313|Proteomes:UP000288675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM103574 {ECO:0000313|EMBL:QAT63762.1,
RC ECO:0000313|Proteomes:UP000288675};
RA Kong H.-J., Jeong S.-Y., Jeong D.-Y.;
RT "Genome sequence of Bacillus glycinifermentans SRCM103574.";
RL Submitted (JAN-2019) 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; CP035232; QAT63762.1; -; Genomic_DNA.
DR EMBL; LT603683; SCA84104.1; -; Genomic_DNA.
DR RefSeq; WP_046129060.1; NZ_LT603683.1.
DR AlphaFoldDB; A0A1C3S8D0; -.
DR GeneID; 82851362; -.
DR KEGG; bgy:BGLY_0281; -.
DR PATRIC; fig|1664069.6.peg.298; -.
DR Proteomes; UP000093092; Chromosome 1.
DR Proteomes; UP000288675; 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 74
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 327 AA; 36119 MW; A639642625433C1E CRC64;
MKEILKERDN AHFRQTRLDD LVEYYRPFSA DGRNAEYIPA LGKIDAKQLG ICVTGSDQTV
MKSGDWDVPF TLQSISKVIS FIAACLTRGI PYVLDRVDAE PTGDAFNSII RLEMHKPGKP
FNPMINAGAL TIASMLPGDS ARDKIETLYA LIEKMIGKRP VINEDVFRSE WETAHRNRAL
AYYLKETGFL EDGVEKTLEV YLKQCAMEGN TEDIAMIGMI LANDGYHPFS HEQIIPKNVA
RLTKALMLTC GMYNASGKFA AFVGVPAKSG VSGGIMCAVP ASFKRKEPFQ HGCGIGIYGP
AIDEYGNSLT GGMLLKQLAQ EWDLSIF
//
