ID   GLSA_LEGPC              Reviewed;         310 AA.
AC   A5IAB4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
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};
GN   OrderedLocusNames=LPC_0319;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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; CP000675; ABQ54314.1; -; Genomic_DNA.
DR   RefSeq; WP_011945486.1; NZ_JAPMSS010000003.1.
DR   AlphaFoldDB; A5IAB4; -.
DR   SMR; A5IAB4; -.
DR   KEGG; lpc:LPC_0319; -.
DR   HOGENOM; CLU_027932_1_0_6; -.
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   Hydrolase.
FT   CHAIN           1..310
FT                   /note="Glutaminase"
FT                   /id="PRO_1000079074"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         118
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   310 AA;  33893 MW;  03B5AE9D78CF47A1 CRC64;
     MSSKLLTIQL LEELVHAAEL NQEGKTADYI PELANVNQEL TAIAVQPLGE KTLAYSNNPL
     HPVTLQSTGK MIPLIGLLEE FGADQLFEWV KVEPSGDDFA SITRLEQFGP KPSNPMLNAG
     AIALCSRIPG VGEQQFRWLE HWVQKLFNQR LSINPLVFAS EKRTGNRNRA LAYLLKSRNN
     LGADVHETLD LYFALCSYEA MLDQMLYLPA VLANRGQDPD TGEQILSIET CKITLAIMAT
     CGLYDETGTH MVKTGMPAKS GVSGYTIAVV PGKAGIVVLS PRVNAKGNSI RGEIMLEGLS
     KAMGWHFALP
//