ID A0A2I1MAR1_9FIRM Unreviewed; 310 AA.
AC A0A2I1MAR1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, 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 ECO:0000313|EMBL:PKZ17226.1};
GN ORFNames=CYJ34_00530 {ECO:0000313|EMBL:PKZ17226.1}, NCTC9810_01243
GN {ECO:0000313|EMBL:SUU92896.1};
OS Anaerococcus octavius.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=54007 {ECO:0000313|EMBL:PKZ17226.1, ECO:0000313|Proteomes:UP000234335};
RN [1] {ECO:0000313|EMBL:PKZ17226.1, ECO:0000313|Proteomes:UP000234335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0119 {ECO:0000313|EMBL:PKZ17226.1,
RC ECO:0000313|Proteomes:UP000234335};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SUU92896.1, ECO:0000313|Proteomes:UP000255124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC9810 {ECO:0000313|EMBL:SUU92896.1,
RC ECO:0000313|Proteomes:UP000255124};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; PKGS01000001; PKZ17226.1; -; Genomic_DNA.
DR EMBL; UFTA01000002; SUU92896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1MAR1; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000234335; Unassembled WGS sequence.
DR Proteomes; UP000255124; 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}.
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 310 AA; 34370 MW; 1D8CB2CC44F959BA CRC64;
MLYKRDFIDQ RIKSVIRTSE SCIGEGKVAS YIPELANVNP DNFALSITSV TGESFNYGNY
DYDFSIQSIC KVLLLIMALH DNDPEAVYNK VGSEPTKYEF NSLVPITDKA SNPFINAGAI
TTASMILGNS VDDKFDRILD YYKKLSKHEK AYLMEEVYSS EMETTDRNKA IAYYLKSKEI
FDDDPEMVLD LYIRACSIST NVVGLSRMGA VLANKGFEID SHYNLLSKSE VQIVLSQMAT
CGMYEKSGRY LMNVGIPSKS GVSGGILGVV PGVCGIGVYS PRLDETGNSV RGKEIFNMLG
QELDLSIFIH
//
