ID   GLSA2_BRADU             Reviewed;         624 AA.
AC   Q89KV2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Glutaminase 2;
DE            EC=3.5.1.2;
GN   Name=glsA2; OrderedLocusNames=bll4798;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR   EMBL; BA000040; BAC50063.1; -; Genomic_DNA.
DR   RefSeq; NP_771438.1; NC_004463.1.
DR   RefSeq; WP_011087566.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89KV2; -.
DR   SMR; Q89KV2; -.
DR   STRING; 224911.AAV28_21285; -.
DR   EnsemblBacteria; BAC50063; BAC50063; BAC50063.
DR   GeneID; 64024552; -.
DR   KEGG; bja:bll4798; -.
DR   PATRIC; fig|224911.44.peg.4637; -.
DR   eggNOG; COG2066; Bacteria.
DR   eggNOG; COG2905; Bacteria.
DR   HOGENOM; CLU_027932_2_0_5; -.
DR   InParanoid; Q89KV2; -.
DR   OrthoDB; 9788822at2; -.
DR   PhylomeDB; Q89KV2; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006543; P:glutamine catabolic process; IBA:GO_Central.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR015868; Glutaminase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   Pfam; PF01740; STAS; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..624
FT                   /note="Glutaminase 2"
FT                   /id="PRO_0000110598"
FT   DOMAIN          355..466
FT                   /note="STAS"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..325
FT                   /note="Glutaminase"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         491..608
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   624 AA;  67583 MW;  75646994C0FF9DAC CRC64;
     MDTQPIRLPS VAGATRSAGY PTRPPLRRFL TDCHEEFRGD SSGELADYIP ELKRANPDHF
     GIALVTIDGH VYEVGDSAVP FTIQSVSKAF VFALALETVG EERVSATIGV EPSGEAFNSI
     RLTNDNRPFN PMVNAGAIAC SGLIYEVDGK GAFERVRSKL SEFAGRELGV DEAVHASETA
     TGNRNRAIAW LLRNYAVLPD DVDAVLDVYF RQCAILVTAR DLAVMAATLA NRGINPVTGA
     QVITPHIVAR TLSVMTSSGM YDYAGEWTYR VGIPAKSGVG GGIVAALPSQ LGLGTFSPLL
     DNHFNSVRGL KVCEALSARF DLHMLNRNAD VRTSVMADYD VYGISSRRSR QPHEQQILDE
     RHSDIRIVEL VGALNFGTID YVTRRLTSEP PNAPLLIIDF RRVPDITAAG AELLGETLTA
     LGNANVTTIL SGLEEASAVW AAIAARTGDP RRLRRFALLD DAIEWAEDQV IYRFGGFTDV
     KESVHLGEQA LLAELDTDEI AAIVKLSTTR HYTAGQRVIA AGAPANSLFF LQSGMVSVKL
     RSGVRLASLG PGMEFGEMAI LERTRSADVF ADTPVACLEL PLDSFADYRR LHPETALKIM
     RNLAAILARR LVAANAKVDL LSAY
//