ID   GLSA_CORGL              Reviewed;         413 AA.
AC   Q8NMT3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glutaminase;
DE            EC=3.5.1.2;
GN   Name=glsA; OrderedLocusNames=Cgl2482, cg2728;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB99875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB99875.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX927155; CAF21143.1; -; Genomic_DNA.
DR   RefSeq; NP_601682.1; NC_003450.3.
DR   RefSeq; WP_003860838.1; NC_006958.1.
DR   AlphaFoldDB; Q8NMT3; -.
DR   SMR; Q8NMT3; -.
DR   STRING; 196627.cg2728; -.
DR   KEGG; cgb:cg2728; -.
DR   KEGG; cgl:Cgl2482; -.
DR   PATRIC; fig|196627.13.peg.2414; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_0_0_11; -.
DR   OMA; RNPMINS; -.
DR   Proteomes; UP000000582; 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..413
FT                   /note="Glutaminase"
FT                   /id="PRO_0000110606"
FT   DOMAIN          316..413
FT                   /note="STAS"
FT   REGION          23..307
FT                   /note="Glutaminase"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  44748 MW;  91ADD397B9FFE473 CRC64;
     MLTMPIPEYL HEILDDVRDT TSGELADYIP ELKSADPNPL AVALCTVNGH IYSAGDDDIE
     FTMQSISKPF AYALALQECG FDEVSASVAL EPSGEAFNEL SLDGENRPMN PMINAGAIAI
     NQLINGSDST VEDRVEKIRH YFSELAGREL TIDRVLAESE LAGADRNLSI AHMLRNYGVI
     EDEAHDAVLS YTLQCAIKVT TRDLAVMTAT LAAGGTHPIT GKKLLDARVC RLTLSVMASA
     GMYDEAGQWL STVGIPAKSG VAGGLIGILP GQLGIATFSP RLNPKGNSVR GVKIFKQLSD
     DMGLHLMSTE QVSGHAVRSI TRDGDTTFIQ MQGAMNFSAS ESFLHAIVEH NFEGTEVVLD
     LTRVLSFHPV AIRMIKEGLK RIRDAGFEVF ILDPDDVLPD FMFSDGTICK ERV