ID   GLSA_PSEA7              Reviewed;         302 AA.
AC   A6V7F4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 64.
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=PSPA7_3635;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABR84204.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000744; ABR84204.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_034000544.1; NC_009656.1.
DR   AlphaFoldDB; A6V7F4; -.
DR   SMR; A6V7F4; -.
DR   EnsemblBacteria; ABR84204; ABR84204; PSPA7_3635.
DR   KEGG; pap:PSPA7_3635; -.
DR   HOGENOM; CLU_027932_1_1_6; -.
DR   OrthoDB; 1288854at2; -.
DR   Proteomes; UP000001582; 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.
FT   CHAIN           1..302
FT                   /note="Glutaminase"
FT                   /id="PRO_0000336035"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   302 AA;  33027 MW;  3F9DFC4646FE2DFA CRC64;
     MQQLLNEILD EVRPLIGRGK VADYIPALAG VEPDQLGIAV YSRDGELFHA GDALRPFSIQ
     SISKVFSLVQ AIQHSGEDIW QRLGHEPSGQ PFNSLVQLEF ERGRPRNPFI NAGALVICDI
     NQSRFAAPAQ SMRDFVRRLC GNPEVVSDSV VARSEYQHRS RNAAAAYLMK SFGNFHNDVE
     AVLLSYFHHC ALRMSCVDLA RAFCFLADKG FCKHSGEQVL NERQTKQVNA IMATSGLYDE
     AGNFAYRVGL PGKSGVGGGI IAVVPGRFTV CVWSPELNGA GNSLAGIAAL EKLSERIGWS
     IF