ID   GLSA_RHIWR              Reviewed;         318 AA.
AC   A5VA34;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Swit_2796;
OS   Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS   105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Rhizorhabdus.
OX   NCBI_TaxID=392499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL   Submitted (MAY-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000699; ABQ69150.1; -; Genomic_DNA.
DR   RefSeq; WP_012049000.1; NC_009511.1.
DR   AlphaFoldDB; A5VA34; -.
DR   SMR; A5VA34; -.
DR   STRING; 392499.Swit_2796; -.
DR   EnsemblBacteria; ABQ69150; ABQ69150; Swit_2796.
DR   KEGG; swi:Swit_2796; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_1_5; -.
DR   OMA; RPRNPFI; -.
DR   OrthoDB; 1288854at2; -.
DR   Proteomes; UP000001989; 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..318
FT                   /note="Glutaminase"
FT                   /id="PRO_0000336041"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   318 AA;  33703 MW;  1AD368F661EC78C6 CRC64;
     MPVTVAPDLQ AIVDRIAAEM AGREERGKVA DYIPGLARVD PKHFGIAVAT HDGRMFAAGD
     ADMAFSIQSV SKVFALTIAL GKVGDALWKR VGREPSGNAF NSIVQLEAEQ GIPRNPFINA
     GAIVVSDVVL AGHAPKEAIG EILRFVRDLA GDDGIVVDDE VAQGEADTGF RNAALANYMR
     SFGNILHPVD QVLGVYFHQC ALAMSCRQLA RAGRFLMHEG QHPDTGFNIV SPMRARRINA
     LMMLCGHYDG SGEFAFRVGI PGKSGVGGGI LCVVPGIASI AVWSPGLNER GNSTLGSLAL
     ERLAAATGWS VFNQREPG