ID   GLSA1_SHIFL             Reviewed;         310 AA.
AC   Q83SE1;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Glutaminase 1 {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA1 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   OrderedLocusNames=SF0430, S0437;
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; AAN42085.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15962.1; -; Genomic_DNA.
DR   RefSeq; NP_706378.1; NC_004337.2.
DR   RefSeq; WP_000883028.1; NZ_WPGW01000015.1.
DR   AlphaFoldDB; Q83SE1; -.
DR   SMR; Q83SE1; -.
DR   STRING; 198214.SF0430; -.
DR   PaxDb; 198214-SF0430; -.
DR   GeneID; 1027752; -.
DR   KEGG; sfl:SF0430; -.
DR   KEGG; sfx:S0437; -.
DR   PATRIC; fig|198214.7.peg.492; -.
DR   HOGENOM; CLU_027932_1_0_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:SF48; GLUTAMINASE 1; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Acetylation; Hydrolase; Reference proteome.
FT   CHAIN           1..310
FT                   /note="Glutaminase 1"
FT                   /id="PRO_0000110624"
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"
FT   MOD_RES         294
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   310 AA;  32875 MW;  98EE622AABECA521 CRC64;
     MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY
     RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA
     IATTSLINAE NAEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY
     LYCDAMEACD VYTRQCSTLI NTVELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM
     EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEEGNSV RGQKMVASVA
     KQLGYNVFKG
//