ID A0A1S2RDH4_9BACI Unreviewed; 309 AA.
AC A0A1S2RDH4;
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_03225 {ECO:0000313|EMBL:OIK16649.1};
OS Bacillus sp. MUM 116.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK16649.1, ECO:0000313|Proteomes:UP000180019};
RN [1] {ECO:0000313|EMBL:OIK16649.1, ECO:0000313|Proteomes:UP000180019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 116 {ECO:0000313|EMBL:OIK16649.1,
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|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:OIK16649.1}.
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DR EMBL; MLYR01000014; OIK16649.1; -; Genomic_DNA.
DR RefSeq; WP_071354279.1; NZ_MLYR01000014.1.
DR AlphaFoldDB; A0A1S2RDH4; -.
DR STRING; 1678002.BIV60_03225; -.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000180019}.
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; 33759 MW; 19410D0B949F6F1B CRC64;
MPCQKNEELK LLVKEAKACT KNGKVADYIP ELGKANPNDL SIAIHYPDGR CTSAGDIDKK
FTLQSISKVI SLALVLMERG SAYVFERVGM EPTGDPFNSI AKLETMAPAK PLNPMINAGA
LVVTHMIKGD TVEERFNRLL TFIQELVGDT IIGYCEKVAR SEFETADLNR ALCYFLKQHN
IIYEDVETLL DLYTKQCAIE MNCLDLARIG MIFAMDGVDP FTGKKIMPDD VARICKTFMV
TCGMYNASGE FAIKIGIPAK SGVSGGIMGA VPGKFGIGIF GPALDEKGNS VAGIKLLELL
SKNYRLSMF
//
