ID   GLSA_CLOB6              Reviewed;         305 AA.
AC   C3L2L2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=CLJ_B3035;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-2008) 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; CP001083; ACQ54791.1; -; Genomic_DNA.
DR   RefSeq; WP_012721317.1; NC_012658.1.
DR   AlphaFoldDB; C3L2L2; -.
DR   SMR; C3L2L2; -.
DR   EnsemblBacteria; ACQ54791; ACQ54791; CLJ_B3035.
DR   KEGG; cbi:CLJ_B3035; -.
DR   HOGENOM; CLU_027932_1_0_9; -.
DR   OMA; RPRNPFI; -.
DR   Proteomes; UP000002333; 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..305
FT                   /note="Glutaminase"
FT                   /id="PRO_1000205061"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         113
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         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   305 AA;  33291 MW;  D6D60503E928054B CRC64;
     MNRLFKTIIE NNRKWVSEGK VASYIPELSK MDKNLLGISV CTLGGEEYWE GDAEVKFTIQ
     SISKIVTLML AIIDNGEDYV FSKVGMEPTE TAFNSIVNLE AKESHKPINP MINAGAIVVA
     SMVAGKDSDE KFDRILKFTR KISGNNNIDI NLNVYKSEKE TGHRNRALAY FMKSTGALKG
     NVEEILDVYF KQCSIEITCK DLARIGVMLA NDGVSPYTGD RIVPRHVARI VKTIMVTCGM
     YDASGNFAVH IGIPAKSGVG GGIVACAPRR MGIGVLGTAL DEKGNSIAGT KILEELSKQL
     DLSIF