ID   GLSA_SALTY              Reviewed;         308 AA.
AC   Q8ZPI2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313}; OrderedLocusNames=STM1525;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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:0000255|HAMAP-Rule:MF_00313};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00313}.
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DR   EMBL; AE006468; AAL20444.1; -; Genomic_DNA.
DR   RefSeq; NP_460485.1; NC_003197.2.
DR   RefSeq; WP_000090081.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPI2; -.
DR   SMR; Q8ZPI2; -.
DR   STRING; 99287.STM1525; -.
DR   PaxDb; Q8ZPI2; -.
DR   EnsemblBacteria; AAL20444; AAL20444; STM1525.
DR   GeneID; 1253043; -.
DR   KEGG; stm:STM1525; -.
DR   PATRIC; fig|99287.12.peg.1613; -.
DR   HOGENOM; CLU_027932_1_1_6; -.
DR   OMA; RPRNPFI; -.
DR   PhylomeDB; Q8ZPI2; -.
DR   BioCyc; SENT99287:STM1525-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006543; P:glutamine catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.710.10; -; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   PANTHER; PTHR12544; PTHR12544; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..308
FT                   /note="Glutaminase"
FT                   /id="PRO_0000110622"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   308 AA;  33597 MW;  4259F8551ED1413F CRC64;
     MARAMDNAIL ETILQRVRPL IGQGKVADYI PALASVEGSK LGIAICTVDG QHYQAGDAHE
     RFSIQSISKV LSLVVAMRHY PEEEIWQRVG KDPSGSPFNS LVQLEMEQGI PRNPFINAGA
     LVVCDMLQGR LSAPRQRMLE VVRALCGVSD ITYDATVARS EFEHSARNAA IAWLMKSFGN
     FHHDVPTVLQ NYFHYCALKM SCMELARTFV FLANQGEAFH LDEPVVTPMQ ARQINALMAT
     SGMYQNAGEF AWRVGLPAKS GVGGGIVAIV PHEMAIAVWS PELDPAGNSL AGIAALEQLT
     QTLGRSVY