ID   GLSA1_BRADU             Reviewed;         613 AA.
AC   Q89NA7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Glutaminase 1;
DE            EC=3.5.1.2;
GN   Name=glsA1; OrderedLocusNames=bll3935;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; 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; BAC49200.1; -; Genomic_DNA.
DR   RefSeq; NP_770575.1; NC_004463.1.
DR   RefSeq; WP_011086712.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89NA7; -.
DR   SMR; Q89NA7; -.
DR   STRING; 224911.27352196; -.
DR   EnsemblBacteria; BAC49200; BAC49200; BAC49200.
DR   GeneID; 64023666; -.
DR   KEGG; bja:bll3935; -.
DR   PATRIC; fig|224911.44.peg.3628; -.
DR   eggNOG; COG2066; Bacteria.
DR   eggNOG; COG2905; Bacteria.
DR   HOGENOM; CLU_027932_2_1_5; -.
DR   InParanoid; Q89NA7; -.
DR   OMA; WAEDQIV; -.
DR   PhylomeDB; Q89NA7; -.
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   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 3.30.750.24; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR015868; Glutaminase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR12544; PTHR12544; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 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..613
FT                   /note="Glutaminase 1"
FT                   /id="PRO_0000110597"
FT   DOMAIN          345..457
FT                   /note="STAS"
FT   REGION          33..315
FT                   /note="Glutaminase"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         480..595
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   613 AA;  66635 MW;  2F7F6A35D48DA118 CRC64;
     MTPPPASAWT RSKPPLLRFL DTCLNEFSAE TSGAVADYIP ELGNADPAYF GISLATLDGH
     VYEVGDSRVP FTIQSMSKPF VFALALDLLG AGRVESAIGV EPSGDPFNSI RLNSDNHPFN
     PMVNAGAIAC TGLIYDSKGA EAFEQIRLAL SRFAGRDLAV DEAVYSSESQ TGDRNRAIGY
     LLKTNAVISD NVAAVLDVYF RQCAVLVTAR DIAVMAATLA NRGINPVTGE QVMSAYAISR
     TLSVMTSSGM YDYAGEWIYR IGIPAKSGVG GGILAALPAR LGLGSYSPKL DKHGNSVRGI
     KVCEALSSHY DLHMLNRSDD ARNAVIADYD IGKSPSRRVR RAQEREILAA HEQEVRIIEL
     VGTLSLSAVD YVSRRLAGRP RPQFVIFDLH RVTSTTRAGA RLVAEAFEEL AALNVTVVLS
     GVRRASKEWN TLREWTAELK NVRDFYLLDT AIEWAEDQIV YRYGGSIDFH ETTELAEQPL
     LEGLSADELA ELGAICTIRT YQSGAKILTT GDPADALFFL RSGAVHVTLP DGVRLATLTA
     GMAFGEMALL EQTRSADVFA DMAATAFEAP LKDFERFREQ HPRASERIMR NLAQLLADRL
     IVANAKVDIL TST