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GLSA_CITK8
ID   GLSA_CITK8              Reviewed;         308 AA.
AC   A8AGR2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313}; OrderedLocusNames=CKO_01543;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV12675.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV12675.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130337.1; NC_009792.1.
DR   AlphaFoldDB; A8AGR2; -.
DR   SMR; A8AGR2; -.
DR   STRING; 290338.CKO_01543; -.
DR   EnsemblBacteria; ABV12675; ABV12675; CKO_01543.
DR   GeneID; 45135607; -.
DR   KEGG; cko:CKO_01543; -.
DR   HOGENOM; CLU_027932_1_1_6; -.
DR   OrthoDB; 1288854at2; -.
DR   Proteomes; UP000008148; 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; -; 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; SSF56601; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..308
FT                   /note="Glutaminase"
FT                   /id="PRO_0000336025"
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;  33573 MW;  7BA455056831DFE3 CRC64;
     MARAMDNSIL ETILQQVRPL IGQGKVADYI PALASVDGSK LGIAICTVDG QYYQAGDAQE
     RFSIQSISKV LSLVVAMRHY PEEEIWQRVG KDPSGSPFNS LVQLELEQGI PRNPFINAGA
     LVVCDMLQGR LSAPRQRMLE VVRALSGVSD IAYDVTVARS EFEHSARNAA IAWLMKSFGN
     FQHDVTTVLQ NYFHYCALKM SCAELARTFV FLARQGQAFH LDEPVVTSMQ ARQINALMAT
     SGMYQNAGEF AWRVGLPAKS GVGGGIVAIV PHEMAIAVWS PELDPAGNSL AGIAVLEQLT
     QQLGRSVY
 
 
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