ID   GLSA_PSEU5              Reviewed;         302 AA.
AC   A4VFZ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=PST_0190;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP77897.1; -; Genomic_DNA.
DR   RefSeq; WP_011911436.1; NC_009434.1.
DR   AlphaFoldDB; A4VFZ6; -.
DR   SMR; A4VFZ6; -.
DR   STRING; 379731.PST_0190; -.
DR   EnsemblBacteria; ABP77897; ABP77897; PST_0190.
DR   KEGG; psa:PST_0190; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_1_6; -.
DR   OMA; RPRNPFI; -.
DR   Proteomes; UP000000233; 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..302
FT                   /note="Glutaminase"
FT                   /id="PRO_1000048347"
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;  32726 MW;  E018C507A7657E3B CRC64;
     MHALLQEILD EVRPLLGRGR VADYIPALAD VPADQLGIAV CSAEGELFEA GDARTPFSIQ
     SISKVFSLVQ AIGHRGESLW ERLGHEPSGQ PFNSLVQLEF ERGRPRNPFI NAGALVICDV
     NQSRFATPEL SMRDFVRHLS GNPLIVSDTK VAESEYQHRA RNAAMAYLMQ AFGNFHNDVE
     AVLRSYFHHC ALRMNCVDLA RAFGFLARDG ICPQGGEAVL SPRQTKQVNA IMATSGLYDE
     AGNFAYRVGL PGKSGVGGGI VAVVPGRFTV CVWSPELNAA GNSLIGMAAL EALSQRIGWS
     VF