ID GLSA2_BACCR Reviewed; 326 AA. AC Q81BN7; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 101. 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}; GN OrderedLocusNames=BC_3115; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB RC 9373 / NCTC 2599 / NRRL B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G., RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus RT anthracis."; RL Nature 423:87-91(2003). 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; AE016877; AAP10058.1; -; Genomic_DNA. DR RefSeq; NP_832857.1; NC_004722.1. DR RefSeq; WP_000588648.1; NZ_CP034551.1. DR AlphaFoldDB; Q81BN7; -. DR SMR; Q81BN7; -. DR STRING; 226900.BC_3115; -. DR KEGG; bce:BC3115; -. DR PATRIC; fig|226900.8.peg.3197; -. DR HOGENOM; CLU_027932_1_0_9; -. DR OrthoDB; 9788822at2; -. DR Proteomes; UP000001417; 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 3: Inferred from homology; KW Hydrolase; Reference proteome. FT CHAIN 1..326 FT /note="Glutaminase 2" FT /id="PRO_0000110591" FT BINDING 73 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 125 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 176 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 252 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 270 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 326 AA; 35856 MW; 24E302EF2E8F56A1 CRC64; MIKDSSVQVE GQEKVCLDQW VAHYRAYAAK GRSASYIPAL GEINVSQLGI CIVKPDGTMI KSGDWEIPFT LQSISKVIGF IAACLSRGIS YVLERVDVEP TGDAFNSIIR LEIHKPGKPF NPMINAGAIT IASLLPGTSV QEKLESLYVL IEKMIEKRPA INEIVFQSEW ETAHRNRALA YYLKENGFLE SDVEETLEVY LKQCSIEINT EDIALIGLIL AHDGYHPIRK EQVLPKEVAR LTKALMLTCG MYNASGKFAA FIGLPAKSGV SGGIMTLVPS KSRKDLSFQD GCGIGIYGPA IDEYGNSLPG IMLLEHIAKE WDLSIF //