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