ID GLSA1_BACCR Reviewed; 309 AA. AC Q81IB3; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Glutaminase 1 {ECO:0000255|HAMAP-Rule:MF_00313}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313}; GN Name=glsA1 {ECO:0000255|HAMAP-Rule:MF_00313}; GN OrderedLocusNames=BC_0481; 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; AAP07519.1; -; Genomic_DNA. DR RefSeq; NP_830318.1; NC_004722.1. DR RefSeq; WP_001149861.1; NZ_CP034551.1. DR AlphaFoldDB; Q81IB3; -. DR SMR; Q81IB3; -. DR STRING; 226900.BC_0481; -. DR KEGG; bce:BC0481; -. DR PATRIC; fig|226900.8.peg.454; -. 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:SF29; GLUTAMINASE; 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..309 FT /note="Glutaminase 1" FT /id="PRO_0000110590" 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; 34093 MW; E097269FD8CB6D9C CRC64; MQCIETNNLQ QLLEQVKPYT KKGKLATYIP ELGNANPDDL GIAIFHKETE YIHAGNSQTL FTLQSISKVI TLALALLDRG EEYVFSKVGM EPTGDPFNSI IKLETTSPSK PLNPMINAGA LAITSMLEGK DNEEKMERIL HFVREITDNP TINYSSKVAD SELETAYLNR SLCYYMKQNG IIDCDIEELM DLYTRQCAVE VNCIDLARIG LIFAMDGYDP YKKKQIIPKH ITKICKTFMV TCGMYNESGE FAIRVGIPAK SGVAGGIFGC VKGDMGIGIF GPALDANGNS IAGFKILELL SAQEGWSIF //