ID   GLSA1_BACSU             Reviewed;         327 AA.
AC   O31465;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Glutaminase 1;
DE            EC=3.5.1.2;
GN   Name=glsA1; Synonyms=glsA, ybgJ; OrderedLocusNames=BSU02430;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, AND GENE NAME.
RC   STRAIN=168;
RX   PubMed=15995196; DOI=10.1128/jb.187.14.4813-4821.2005;
RA   Satomura T., Shimura D., Asai K., Sadaie Y., Hirooka K., Fujita Y.;
RT   "Enhancement of glutamine utilization in Bacillus subtilis through the
RT   GlnK-GlnL two-component regulatory system.";
RL   J. Bacteriol. 187:4813-4821(2005).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP   5-OXO-L-NORLEUCINE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RX   PubMed=18459799; DOI=10.1021/bi800097h;
RA   Brown G., Singer A., Proudfoot M., Skarina T., Kim Y., Chang C.,
RA   Dementieva I., Kuznetsova E., Gonzalez C.F., Joachimiak A., Savchenko A.,
RA   Yakunin A.F.;
RT   "Functional and structural characterization of four glutaminases from
RT   Escherichia coli and Bacillus subtilis.";
RL   Biochemistry 47:5724-5735(2008).
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:0000269|PubMed:18459799};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27.6 mM for glutamine {ECO:0000269|PubMed:18459799};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18459799}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR   EMBL; AB006424; BAA33141.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12037.1; -; Genomic_DNA.
DR   PIR; D69751; D69751.
DR   RefSeq; NP_388125.1; NC_000964.3.
DR   RefSeq; WP_003234829.1; NZ_JNCM01000030.1.
DR   PDB; 1MKI; X-ray; 2.00 A; A/B=1-327.
DR   PDB; 2OSU; X-ray; 2.29 A; A/B=1-327.
DR   PDB; 3AGF; X-ray; 2.60 A; A/B=1-327.
DR   PDB; 3BRM; X-ray; 2.29 A; A/B=1-327.
DR   PDBsum; 1MKI; -.
DR   PDBsum; 2OSU; -.
DR   PDBsum; 3AGF; -.
DR   PDBsum; 3BRM; -.
DR   AlphaFoldDB; O31465; -.
DR   SMR; O31465; -.
DR   STRING; 224308.BSU02430; -.
DR   DrugBank; DB04522; Dexfosfoserine.
DR   DrugBank; DB01942; Formic acid.
DR   PaxDb; 224308-BSU02430; -.
DR   DNASU; 938416; -.
DR   EnsemblBacteria; CAB12037; CAB12037; BSU_02430.
DR   GeneID; 938416; -.
DR   KEGG; bsu:BSU02430; -.
DR   PATRIC; fig|224308.179.peg.250; -.
DR   eggNOG; COG2066; Bacteria.
DR   InParanoid; O31465; -.
DR   OrthoDB; 9788822at2; -.
DR   PhylomeDB; O31465; -.
DR   BioCyc; BSUB:BSU02430-MONOMER; -.
DR   BRENDA; 3.5.1.2; 658.
DR   BRENDA; 4.3.3.6; 658.
DR   SABIO-RK; O31465; -.
DR   EvolutionaryTrace; O31465; -.
DR   PRO; PR:O31465; -.
DR   Proteomes; UP000001570; 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   Gene3D; 1.10.1500.10; -; 1.
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:SF32; GLUTAMINASE 1; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..327
FT                   /note="Glutaminase 1"
FT                   /id="PRO_0000110594"
FT   BINDING         74
FT                   /ligand="substrate"
FT   BINDING         126
FT                   /ligand="substrate"
FT   BINDING         170
FT                   /ligand="substrate"
FT   BINDING         177
FT                   /ligand="substrate"
FT   BINDING         201
FT                   /ligand="substrate"
FT   BINDING         253
FT                   /ligand="substrate"
FT   BINDING         271
FT                   /ligand="substrate"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           26..31
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:2OSU"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           76..88
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           90..94
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           110..114
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           126..135
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           141..156
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           164..173
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           175..186
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           194..205
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           211..222
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   TURN            228..231
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           237..250
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           256..262
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   TURN            281..284
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   TURN            288..291
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          293..298
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:1MKI"
FT   HELIX           309..322
FT                   /evidence="ECO:0007829|PDB:1MKI"
SQ   SEQUENCE   327 AA;  36187 MW;  BE3A1C2366460287 CRC64;
     MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG ICVLEPDGTM
     IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE PTGDAFNSII RLEINKPGKP
     FNPMINAGAL TIASILPGES AYEKLEFLYS VMETLIGKRP RIHEEVFRSE WETAHRNRAL
     AYYLKETNFL EAEVEETLEV YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA
     KLAKALMLTC GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP
     AIDEYGNSLT GGMLLKHMAQ EWELSIF
//