ID GLSA_ALKMQ Reviewed; 305 AA. AC A6TU96; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 81. 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=Amet_3642; OS Alkaliphilus metalliredigens (strain QYMF). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=293826; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF; RX PubMed=27811105; DOI=10.1128/genomea.01226-16; RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., RA Richardson P., Fields M.W.; RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated RT leachate ponds."; RL Genome Announc. 4:0-0(2016). 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; CP000724; ABR49764.1; -; Genomic_DNA. DR RefSeq; WP_012064724.1; NC_009633.1. DR AlphaFoldDB; A6TU96; -. DR SMR; A6TU96; -. DR STRING; 293826.Amet_3642; -. DR KEGG; amt:Amet_3642; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_0_9; -. DR OrthoDB; 9788822at2; -. DR Proteomes; UP000001572; 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..305 FT /note="Glutaminase" FT /id="PRO_0000336021" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 241 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 305 AA; 33617 MW; E81102CDDBE3EB6D CRC64; MNEQLQKILD TNRHHIQGGQ LPTYIPELSK ANKEALGIYV ADLDGNEYGV GDYEYPFTIQ SISKVVTLLL ALSDRGEKYV FDKVGMEPTG DPFNSMMKLE VVRPSKPFNP MINAGAIAVT SMIKGDSQKE RLERILGFFR QLTENPNLQV NQSVYRSEKI TGDRNRSMAY FMKDVGIMQN DIESDLDLYF NQCSIEVTCK DIAKIGRFLA NGGVLFETGQ QLIDEKYIKM AEAFMVTCGM YNASGEFAIK VGIPAKSGVG GGIMASVPKK MGIGVVGPSL DEKGNSIAGV RVLQKMAEDY GLSIF //