ID   GLSA_ALKOO              Reviewed;         305 AA.
AC   A8MIB3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Clos_2008;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) 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: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; CP000853; ABW19545.1; -; Genomic_DNA.
DR   RefSeq; WP_012159854.1; NC_009922.1.
DR   AlphaFoldDB; A8MIB3; -.
DR   SMR; A8MIB3; -.
DR   STRING; 350688.Clos_2008; -.
DR   EnsemblBacteria; ABW19545; ABW19545; Clos_2008.
DR   KEGG; aoe:Clos_2008; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_1_9; -.
DR   OMA; RPRNPFI; -.
DR   OrthoDB; 1288854at2; -.
DR   Proteomes; UP000000269; Chromosome.
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; -; 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..305
FT                   /note="Glutaminase"
FT                   /id="PRO_0000336022"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   305 AA;  33308 MW;  97B76E03F436237B CRC64;
     MQIELEKILN QNREKIAFGN LPTYIPELTR ANKDALGIYI SQLDGSEFKA GDYDYKFTIQ
     SISKVITLIM ALEDWGAEYI FECVGKEPTG DAFNSMMKLE IVRPSKPFNP MINAGAIAVT
     SKIKGKSPEE RIQRIMDFFK LVTGNPDLKV NESIYMSEKS TGDRNRAMAY FMKDVGVITG
     DVEENLDLYF KQCSIEVTCK DIARIGLFLS SDGVLLETGK QIINPKHSKI AKALMTTCGM
     YNASGEFAIN VGIPAKSGVG GGIMAVVPGK MGIGVIGPSL DEKGNSIAGV GVLEQLSKML
     ELSIF