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Database: UniProt/TrEMBL
Entry: D5C8U5_ENTCC
LinkDB: D5C8U5_ENTCC
Original site: D5C8U5_ENTCC 
ID   D5C8U5_ENTCC            Unreviewed;       308 AA.
AC   D5C8U5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   01-MAY-2013, entry version 20.
DE   RecName: Full=Glutaminase;
DE            EC=3.5.1.2;
GN   Name=glsA; OrderedLocusNames=ECL_01990;
OS   Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 /
OS   NBRC 13535 / NCDC 279-56).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=716541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCDC 279-56;
RX   PubMed=20207761; DOI=10.1128/JB.00067-10;
RA   Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT   "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT   strain ATCC 13047.";
RL   J. Bacteriol. 192:2463-2464(2010).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the glutaminase family.
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DR   EMBL; CP001918; ADF61542.1; -; Genomic_DNA.
DR   RefSeq; YP_003612491.1; NC_014121.1.
DR   EnsemblBacteria; ADF61542; ADF61542; ECL_01990.
DR   GeneID; 9124485; -.
DR   KEGG; enc:ECL_01990; -.
DR   PATRIC; 38454898; VBIEntClo148801_2189.
DR   HOGENOM; HOG000216890; -.
DR   KO; K01425; -.
DR   BioCyc; ECLO716541:GH13-1974-MONOMER; -.
DR   GO; GO:0004359; F:glutaminase activity; IEA:HAMAP.
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; PBP_transp_fold; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
PE   3: Inferred from homology;
KW   Acetylation; Complete proteome; Hydrolase.
FT   BINDING      66     66       Substrate (By similarity).
FT   BINDING     117    117       Substrate (By similarity).
FT   BINDING     161    161       Substrate (By similarity).
FT   BINDING     168    168       Substrate (By similarity).
FT   BINDING     192    192       Substrate (By similarity).
FT   BINDING     244    244       Substrate (By similarity).
FT   BINDING     262    262       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   308 AA;  33681 MW;  78A125B367CFF806 CRC64;
     MAAVIHNEML DEILAQVRPL LGKGKVADYI PALASVSGNK LGIAICTIDG QRYQAGDATE
     RFSIQSISKV LSLVAAMRQY EEEEIWQRVG KDPSGQPFNS LLQLEIEQGK PRNPFINAGA
     LVVCDMLQSR LSAPRQRMLE IVRQLSGVDD IAYDSVVARS EFEHSARNAA IAWLMKSFGN
     FHNDVATVLQ NYFHYCALKM SCVELAQTFL FLAHQGHAPH LDQEVVSPMQ ARQVNALMAT
     SGMYQNAGEF AWRVGLPAKS GVGGGVVAIV PHEMAIAVWS PELDETGNSL AGVAVLEKLT
     QRLGRSVY
//
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