ID A0A1S2REC4_9BACI Unreviewed; 329 AA.
AC A0A1S2REC4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BIV60_02750 {ECO:0000313|EMBL:OIK16804.1};
OS Bacillus sp. MUM 116.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK16804.1, ECO:0000313|Proteomes:UP000180019};
RN [1] {ECO:0000313|EMBL:OIK16804.1, ECO:0000313|Proteomes:UP000180019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 116 {ECO:0000313|EMBL:OIK16804.1,
RC ECO:0000313|Proteomes:UP000180019};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 116.";
RL Submitted (OCT-2016) 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}.
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:OIK16804.1}.
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DR EMBL; MLYR01000010; OIK16804.1; -; Genomic_DNA.
DR RefSeq; WP_071354198.1; NZ_MLYR01000010.1.
DR AlphaFoldDB; A0A1S2REC4; -.
DR STRING; 1678002.BIV60_02750; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000180019; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000180019}.
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 329 AA; 36114 MW; 7D7771EB69265988 CRC64;
MAVAKEIIPF EKQREIFNLD QWVEHYRSYA VKGRCASYIP ALEKANLSQL GVVMVGPDGT
VLKSGECAVS FTLQSISKVI SFIAACLDFG TPYVLDRVDV EPTGDAFNSI IRLEMHKPGR
PFNPMINAGA LTVASLLGGR SPLEKIESFL TLFEKMVGKR PSINEKVFQS EWQTAHRNRA
LAYYLKETGF LESTVEEALE VYLKQCSIEV NSKDIAMIGL VLAYDGFHPI RREQIFPREV
ARLTKALMVT CGMYNASGKF AAHIGLPAKS GVSGGIMAAV PARVSSQDSP FPHGCGIGLY
GPAIDEYGNS VAGSMLLKHI AREWDLNIF
//
