ID   GLSA_COREF              Reviewed;         423 AA.
AC   Q8FMX4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Glutaminase;
DE            EC=3.5.1.2;
GN   Name=glsA; OrderedLocusNames=CE2375;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR   EMBL; BA000035; BAC19185.1; -; Genomic_DNA.
DR   RefSeq; WP_006768381.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FMX4; -.
DR   SMR; Q8FMX4; -.
DR   STRING; 196164.23494218; -.
DR   EnsemblBacteria; BAC19185; BAC19185; BAC19185.
DR   KEGG; cef:CE2375; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_0_0_11; -.
DR   OMA; RNPMINS; -.
DR   OrthoDB; 1288854at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.750.24; -; 2.
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   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR12544; PTHR12544; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..423
FT                   /note="Glutaminase"
FT                   /id="PRO_0000110605"
FT   DOMAIN          321..423
FT                   /note="STAS"
FT   REGION          27..312
FT                   /note="Glutaminase"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   423 AA;  45863 MW;  CDEB65C617F289CB CRC64;
     MTTHPLTMPI PEYFEEILES VRSDVSGEVA QYIPQLKDAD PNPLALAMCT VDGHIYGAGD
     DEHEFTMQSV SKPFAYALAL QEQGPEKVFA TVGLEPSGEA FNELSLDGST NRPMNPMINA
     GAIAVNQLIN GSESSVEDRV EKIRSYFSAL AGRELNIDRQ LSETEIEGAD RNLSIAHMLR
     NYGIIEDDAH DAVLSYTLQC SVKVTARDLA VMTATLAAGG TQPLTGEKLV DARVARLVLS
     TMASAGMYDE AGQWLATVGI PAKSGVSGGL VGVLPGQLGL ATFSPRLNSQ GNPVRGVEIF
     KALSEDMGLH LMSAELLTQH AVRAIEERGD TTVIQLQGAM NFSAAENFLF TVTDHDFTGE
     KVVLDISRVP MFRPMGRRLV KEGLRRIRDN GFKVAIYDPE DILPDFDFSD GTKSPQVDDP
     EEL