ID   GLSA2_SHIFL             Reviewed;         308 AA.
AC   Q83RE2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 116.
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};
GN   OrderedLocusNames=SF1569, S1696;
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43157.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17051.1; -; Genomic_DNA.
DR   RefSeq; NP_707450.1; NC_004337.2.
DR   RefSeq; WP_000257419.1; NZ_WPGW01000096.1.
DR   AlphaFoldDB; Q83RE2; -.
DR   SMR; Q83RE2; -.
DR   STRING; 198214.SF1569; -.
DR   PaxDb; 198214-SF1569; -.
DR   GeneID; 1024764; -.
DR   KEGG; sfl:SF1569; -.
DR   KEGG; sfx:S1696; -.
DR   PATRIC; fig|198214.7.peg.1855; -.
DR   HOGENOM; CLU_027932_1_1_6; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..308
FT                   /note="Glutaminase 2"
FT                   /id="PRO_0000110625"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   308 AA;  33546 MW;  D1A290F0B0C4DF34 CRC64;
     MAVAMDNAIL ENILRQVRPL IGQGKVADYI PALATVDGSR LGIAICTVDG QLFQAGDAQE
     RFSIQSISKV LSLVVAMRHY SEEEIWQRVG KDPSGSPFNS LVQLEMEQGI PRNPFINTGA
     LVVCDMLQGR LSAPRQRMLE VVRGLSGVSD ISYDTVVARS EFEHSARNAA IAWLMKSFGN
     FHHDVTTVLQ NYFHYCALKM SCVELARTFV FLANQGKAIH IDEPVVTPMQ ARQINALMAT
     SGMYQNAGEF AWRVGLPAKS GVGGGIVAIV PHEMAIAVWS PELDDAGNSL AGIAVLEQLT
     KQLGRSVY
//