ID   GLSA2_BACSU             Reviewed;         309 AA.
AC   O07637;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Glutaminase 2 {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA2 {ECO:0000255|HAMAP-Rule:MF_00313}; Synonyms=ylaM;
GN   OrderedLocusNames=BSU14830;
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   Purnelle B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.;
RT   "Bacillus subtilis chromosomal region downstream nprE.";
RL   Submitted (JUN-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   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 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:0000255|HAMAP-Rule:MF_00313,
CC         ECO:0000269|PubMed:18459799};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.6 mM for glutamine {ECO:0000269|PubMed:18459799};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313,
CC       ECO:0000269|PubMed:18459799}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00313}.
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DR   EMBL; Z97025; CAB09718.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13356.1; -; Genomic_DNA.
DR   PIR; C69873; C69873.
DR   RefSeq; NP_389366.1; NC_000964.3.
DR   RefSeq; WP_003245206.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O07637; -.
DR   SMR; O07637; -.
DR   STRING; 224308.BSU14830; -.
DR   PaxDb; 224308-BSU14830; -.
DR   EnsemblBacteria; CAB13356; CAB13356; BSU_14830.
DR   GeneID; 939852; -.
DR   KEGG; bsu:BSU14830; -.
DR   PATRIC; fig|224308.179.peg.1617; -.
DR   eggNOG; COG2066; Bacteria.
DR   InParanoid; O07637; -.
DR   OrthoDB; 9788822at2; -.
DR   PhylomeDB; O07637; -.
DR   BioCyc; BSUB:BSU14830-MONOMER; -.
DR   BRENDA; 3.5.1.2; 658.
DR   SABIO-RK; O07637; -.
DR   PRO; PR:O07637; -.
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; 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:SF29; GLUTAMINASE; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..309
FT                   /note="Glutaminase 2"
FT                   /id="PRO_0000110595"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   309 AA;  34012 MW;  E1DFEF1A0723C1A5 CRC64;
     MVCQHNDELE ALVKKAKKVT DKGEVASYIP ALAKADKHDL SVAIYYSNNV CLSAGDVEKT
     FTLQSISKVL SLALVLMEYG KDKVFSYVGQ EPTGDPFNSI IKLETVNPSK PLNPMINAGA
     LVVTSLIRGR TVKERLDYLL SFIRRLTNNQ EITYCREVAE SEYSTSMINR AMCYYMKQYG
     IFEDDVEAVM DLYTKQCAIE MNSLDLAKIG SVFALNGRHP ETGEQVISKD VARICKTFMV
     TCGMYNASGE FAIKVGIPAK SGVSGGIMGI SPYDFGIGIF GPALDEKGNS IAGVKLLEIM
     SEMYRLSIF
//