ID   GLSA_CHRFK              Reviewed;         304 AA.
AC   A0M4Z1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
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};
GN   OrderedLocusNames=GFO_2730;
OS   Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803)
OS   (Gramella forsetii).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17595 / CGMCC 1.15422 / KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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}.
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DR   EMBL; CU207366; CAL67686.1; -; Genomic_DNA.
DR   RefSeq; WP_011710589.1; NC_008571.1.
DR   AlphaFoldDB; A0M4Z1; -.
DR   SMR; A0M4Z1; -.
DR   STRING; 411154.GFO_2730; -.
DR   KEGG; gfo:GFO_2730; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_1_10; -.
DR   OrthoDB; 9788822at2; -.
DR   Proteomes; UP000000755; 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; DD-peptidase/beta-lactamase superfamily; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..304
FT                   /note="Glutaminase"
FT                   /id="PRO_0000336028"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   304 AA;  34011 MW;  47492A99A0B17C21 CRC64;
     MDYQQILDTI NDEMSYRDVT GKVASYIPEL AKVDRRKFGM HVYCGDQQHF SFGDSEENFS
     IQSISKVFTL AMAMRLMGED LWDRLDVEPS GDPFNSLTQL EYESGIPRNP FINAGALVIS
     DILVDQLEDP KKELLEFVRK ITGDDNIHYN ETVAASEKST GYRNIALVNY IKALGNIKCD
     VEPIVDFYFY QCSLAMSCSQ LSKAFMIFAN KGRILETDEK ILKPKTVKRI NALMQTCGFY
     DEAGEFSFQV GMPGKSGVGG GIVAIHPDNY SVAVWSPILN ENGNSELGMK ALERFTTLTG
     VSVF
//