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Database: UniProt/SWISS-PROT
Entry: GLSA1_SHIFL
LinkDB: GLSA1_SHIFL
Original site: GLSA1_SHIFL 
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   22-NOV-2017, entry version 89.
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; Proteobacteria; 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.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   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.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC       {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}.
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_NMXZ01000017.1.
DR   ProteinModelPortal; Q83SE1; -.
DR   SMR; Q83SE1; -.
DR   PaxDb; Q83SE1; -.
DR   EnsemblBacteria; AAN42085; AAN42085; SF0430.
DR   EnsemblBacteria; AAP15962; AAP15962; S0437.
DR   GeneID; 1027752; -.
DR   KEGG; sfl:SF0430; -.
DR   KEGG; sfx:S0437; -.
DR   PATRIC; fig|198214.7.peg.492; -.
DR   eggNOG; ENOG4105CSV; Bacteria.
DR   eggNOG; COG2066; LUCA.
DR   HOGENOM; HOG000216890; -.
DR   KO; K01425; -.
DR   OMA; MYTCGMY; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
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   Acetylation; Complete proteome; Hydrolase.
FT   CHAIN         1    310       Glutaminase 1.
FT                                /FTId=PRO_0000110624.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     117    117       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     161    161       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     168    168       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     192    192       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     244    244       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00313}.
FT   MOD_RES     294    294       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                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
//
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