ID   GLSA_SHEB9              Reviewed;         304 AA.
AC   A9KXQ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=Sbal195_3193;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP000891; ABX50355.1; -; Genomic_DNA.
DR   RefSeq; WP_006085711.1; NC_009997.1.
DR   AlphaFoldDB; A9KXQ3; -.
DR   SMR; A9KXQ3; -.
DR   GeneID; 11774897; -.
DR   KEGG; sbn:Sbal195_3193; -.
DR   HOGENOM; CLU_027932_1_1_6; -.
DR   Proteomes; UP000000770; 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; 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..304
FT                   /note="Glutaminase"
FT                   /id="PRO_1000079079"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   304 AA;  32782 MW;  D3F89341F113E7A3 CRC64;
     MPELALLEEV VEKVRPLLGQ GKVADYIPAL ASVDAGKLGI AVTTVDGETL GAGDYLEPFS
     IQSISKVFSL TLALTLYEEA EIWSRVGKEP SGHSFNSLVQ VELERGKPRN PFINAGALVI
     ADLLQSRLGA PKHRMLELVR QLSQNDKVSF DKQVADSEYQ HSARNAAIAY LMKSFGNFQG
     DVDTVLRTYF HYCALKMNCA DLSKAMLYLA NRGKSITGTE LISQVQTRQL NALLATSGLY
     DGAGEFAYRV GMPGKSGVGG GIIAVIPGEL SICVWSPELD GNGNSLAGTA MLEHLSQRLG
     RSIF
//