ID GLSA_COREF Reviewed; 423 AA. AC Q8FMX4; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 113. DE RecName: Full=Glutaminase; DE EC=3.5.1.2; GN Name=glsA; OrderedLocusNames=CE2375; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamine + H2O = 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 -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}. 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; BA000035; BAC19185.1; -; Genomic_DNA. DR RefSeq; WP_006768381.1; NC_004369.1. DR AlphaFoldDB; Q8FMX4; -. DR SMR; Q8FMX4; -. DR STRING; 196164.gene:10742812; -. DR KEGG; cef:CE2375; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_0_0_11; -. DR OrthoDB; 9788822at2; -. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006543; P:L-glutamine catabolic process; IEA:TreeGrafter. DR FunFam; 3.40.710.10:FF:000005; Glutaminase; 1. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR Gene3D; 3.30.750.24; STAS domain; 2. DR HAMAP; MF_00313; Glutaminase; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR015868; Glutaminase. DR InterPro; IPR002645; STAS_dom. DR InterPro; IPR036513; STAS_dom_sf. DR NCBIfam; TIGR03814; Gln_ase; 1. DR NCBIfam; NF002134; PRK00971.1-4; 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. DR SUPFAM; SSF52091; SpoIIaa-like; 1. DR PROSITE; PS50801; STAS; 1. PE 3: Inferred from homology; KW Hydrolase; Reference proteome. FT CHAIN 1..423 FT /note="Glutaminase" FT /id="PRO_0000110605" FT DOMAIN 321..423 FT /note="STAS" FT REGION 27..312 FT /note="Glutaminase" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 196 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 423 AA; 45863 MW; CDEB65C617F289CB CRC64; MTTHPLTMPI PEYFEEILES VRSDVSGEVA QYIPQLKDAD PNPLALAMCT VDGHIYGAGD DEHEFTMQSV SKPFAYALAL QEQGPEKVFA TVGLEPSGEA FNELSLDGST NRPMNPMINA GAIAVNQLIN GSESSVEDRV EKIRSYFSAL AGRELNIDRQ LSETEIEGAD RNLSIAHMLR NYGIIEDDAH DAVLSYTLQC SVKVTARDLA VMTATLAAGG TQPLTGEKLV DARVARLVLS TMASAGMYDE AGQWLATVGI PAKSGVSGGL VGVLPGQLGL ATFSPRLNSQ GNPVRGVEIF KALSEDMGLH LMSAELLTQH AVRAIEERGD TTVIQLQGAM NFSAAENFLF TVTDHDFTGE KVVLDISRVP MFRPMGRRLV KEGLRRIRDN GFKVAIYDPE DILPDFDFSD GTKSPQVDDP EEL //