ID GLSA_BRUA2 Reviewed; 317 AA.
AC Q2YK17;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=BAB2_0863;
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ13029.1; -; Genomic_DNA.
DR RefSeq; WP_002967336.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YK17; -.
DR SMR; Q2YK17; -.
DR STRING; 359391.BAB2_0863; -.
DR DNASU; 3827366; -.
DR GeneID; 3827366; -.
DR KEGG; bmf:BAB2_0863; -.
DR PATRIC; fig|359391.11.peg.551; -.
DR HOGENOM; CLU_027932_1_0_5; -.
DR PhylomeDB; Q2YK17; -.
DR Proteomes; UP000002719; Chromosome II.
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:SF48; GLUTAMINASE 1; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..317
FT /note="Glutaminase"
FT /id="PRO_1000048327"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 317 AA; 32463 MW; A5ED37D230E862BD CRC64;
MSSSSDAIKA ALEKGRAAGL SATGGKNADY IPFLASVPSD LFGLAVVTAD GQTFKTGDAD
IAFAIESISK VFTLALVMEE IGPDSVREKV GADPTGLPFN SVIALELHNG KSLSPLVNAG
AIATASLVPG DTADARWNNI LECQCGFAGR RLKLSNEVNQ SEQTTNFHNR AIAWLLYSAG
TCYSDPMEAV DIYTRQCSTL VTATDLATMG ATLAAGGVNP ISGKRMVSAG NVAPILVEMT
MEGLYTALGD WAYTVGLPGK SGVGGGIMAV VPGELAIAAF SPPLDPAGNS VKAMAAVAAV
ADSLGHNLYT TRGKVSS
//
