(data stored in ACNUC7421 zone)

SWISSPROT: GLSA1_ECO57

ID   GLSA1_ECO57             Reviewed;         310 AA.
AC   Q8XD23;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 84.
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=Z0606, ECs0538;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54834.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33961.1; -; Genomic_DNA.
DR   PIR; B90696; B90696.
DR   PIR; F85546; F85546.
DR   RefSeq; NP_308565.1; NC_002695.1.
DR   RefSeq; WP_000883037.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; Q8XD23; -.
DR   SMR; Q8XD23; -.
DR   STRING; 155864.Z0606; -.
DR   EnsemblBacteria; AAG54834; AAG54834; Z0606.
DR   EnsemblBacteria; BAB33961; BAB33961; BAB33961.
DR   GeneID; 914642; -.
DR   KEGG; ece:Z0606; -.
DR   KEGG; ecs:ECs0538; -.
DR   PATRIC; fig|386585.9.peg.645; -.
DR   eggNOG; ENOG4105CSV; Bacteria.
DR   eggNOG; COG2066; LUCA.
DR   HOGENOM; HOG000216890; -.
DR   KO; K01425; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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;
DR   PRODOM; Q8XD23.
DR   SWISS-2DPAGE; Q8XD23.
KW   Acetylation; Complete proteome; Hydrolase.
FT   CHAIN         1    310       Glutaminase 1.
FT                                /FTId=PRO_0000110609.
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;  32844 MW;  9B335D6AA51CB378 CRC64;
     MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTSDG NVYSAGDSDY
     RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA
     IATTSLINAE NAEQRWQRIL HIQQQLAGEL VALSDEVNQS EQTTNFHNRA IAWLLYSAGY
     LYCDAMEACD VYTRQCSTLI NTVELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM
     EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEEGNSV RGQKMVASVA
     KQLGYNVFKG
//

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