ID   GLSA_RHIE6              Reviewed;         309 AA.
AC   B3PPT2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=RHECIAT_CH0002407;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) 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}.
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DR   EMBL; CP001074; ACE91361.1; -; Genomic_DNA.
DR   RefSeq; WP_010024905.1; NC_010994.1.
DR   AlphaFoldDB; B3PPT2; -.
DR   SMR; B3PPT2; -.
DR   EnsemblBacteria; ACE91361; ACE91361; RHECIAT_CH0002407.
DR   GeneID; 45957702; -.
DR   KEGG; rec:RHECIAT_CH0002407; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_1_5; -.
DR   OMA; RPRNPFI; -.
DR   Proteomes; UP000008817; 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.
FT   CHAIN           1..309
FT                   /note="Glutaminase"
FT                   /id="PRO_1000115701"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   309 AA;  33003 MW;  59E24CFDF4176750 CRC64;
     MADLKAILDS IYTDILPRVG EGKVADYIPE LAKVDPRQFG MAIVTVDGKV YRVGDADIAF
     SIQSISKVFM LTLALGKVGE GLWKRVGREP SGSAFNSIVQ LEHESGIPRN PFINAGAIAV
     TDVVMAGHAP REAIGELLRF VRYLADDESI TIDDKVARSE TQTGYRNVAL ANFMRAYRNL
     DHPVDHVLGV YFHQCALSMS CEQLARAGLF LAARGSNPMT GHSVVSPKRA RRINALMLTC
     GHYDGSGDFA YHVGLPGKSG VGGGIFAVAP GIASIAVWSP GLNKVGNSQL GAVALEMLAA
     RTGWSVFGD