ID GLSA_CLOD6 Reviewed; 309 AA. AC Q189A6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313}; GN Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313}; GN OrderedLocusNames=CD630_05580; OS Clostridioides difficile (strain 630) (Peptoclostridium difficile). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae; OC Clostridioides. OX NCBI_TaxID=272563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L., RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a highly RT mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). 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; AM180355; CAJ67391.1; -; Genomic_DNA. DR RefSeq; WP_003417962.1; NZ_JAUPES010000001.1. DR RefSeq; YP_001087034.1; NC_009089.1. DR AlphaFoldDB; Q189A6; -. DR SMR; Q189A6; -. DR STRING; 272563.CD630_05580; -. DR EnsemblBacteria; CAJ67391; CAJ67391; CD630_05580. DR GeneID; 66353055; -. DR KEGG; cdf:CD630_05580; -. DR KEGG; pdc:CDIF630_00671; -. DR PATRIC; fig|272563.120.peg.568; -. DR eggNOG; COG2066; Bacteria. DR OrthoDB; 9788822at2; -. DR PhylomeDB; Q189A6; -. DR BioCyc; PDIF272563:G12WB-670-MONOMER; -. DR Proteomes; UP000001978; Chromosome. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro. 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" FT /id="PRO_1000048333" 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; 33948 MW; 23BA33CA6B2B95EF CRC64; MNTLDETLLK EIISSNKKYT NYGQVASYIP ELKNARRNDL GICIIDSENN LYSAGNCSTK FTIQSISKPI VLAMALMDND WEDVFSNVGM EPSGDPFNSI MKLEINDTKK PCNPMINAGA IVTTSLINGS CLEEKEERML SFFRKLAKND NIGINYDVYK SEKMTGDRNR AMAYLLKSDG FIRGNVEDVL DLYFKQCSIE IDSVDLARIG INLANYGVDI ENGEHLMSEM VSRIVKTFMM TCGMYDASGE FAIKVGIPAK SGVGGGIMAS VPGRMGIGVY GPALDKKGNS VAGVKVLEEL SNKLKLNIF //