ID   GLSA2_CLOPE             Reviewed;         305 AA.
AC   Q8XIW8;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Glutaminase 2 {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA2 {ECO:0000255|HAMAP-Rule:MF_00313}; OrderedLocusNames=CPE1995;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81701.1; -; Genomic_DNA.
DR   RefSeq; WP_003451262.1; NC_003366.1.
DR   AlphaFoldDB; Q8XIW8; -.
DR   SMR; Q8XIW8; -.
DR   STRING; 195102.gene:10491265; -.
DR   PRIDE; Q8XIW8; -.
DR   EnsemblBacteria; BAB81701; BAB81701; BAB81701.
DR   GeneID; 29570643; -.
DR   KEGG; cpe:CPE1995; -.
DR   HOGENOM; CLU_027932_1_0_9; -.
DR   OMA; RPRNPFI; -.
DR   Proteomes; UP000000818; 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..305
FT                   /note="Glutaminase 2"
FT                   /id="PRO_0000110603"
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;  33691 MW;  2951FD6F7A9C8289 CRC64;
     MKNFLESLIE NNRQYVEHGK LASYIPELEK ANKEDLGIYI VTLDGKEVGA GEYDKKFTIQ
     SISKVITLML AILDNGKDRV FSRVGVEPTG DSFNSIVSLE RKPSKKPFNP MVNSGAILTT
     SLIEGDSEEE KFERILEFTR KVTGNDDIQL NEDVYLSEKE TGDRNRALAY FMKSNGVIEG
     NIDDILDLYF KQCSLEVNAK DLARFGAMLA NDGVLPWNGE RVISREICRI IKTIMVTCGM
     YDDSGKFAVH IGIPAKSGVG GGIMAAVPRR MGIGIFGPSL DDKGNSIAGT HVMKDLSEEL
     DLSIF