ID GLSA_NATTJ Reviewed; 308 AA. AC B2A4X5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 80. 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=Nther_0299; OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / OS JW/NM-WN-LF). OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae; OC Natranaerobius. OX NCBI_TaxID=457570; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.; RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN- RT LF."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. 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; CP001034; ACB83897.1; -; Genomic_DNA. DR RefSeq; WP_012446785.1; NC_010718.1. DR AlphaFoldDB; B2A4X5; -. DR SMR; B2A4X5; -. DR STRING; 457570.Nther_0299; -. DR KEGG; nth:Nther_0299; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_0_9; -. DR InParanoid; B2A4X5; -. DR OrthoDB; 9788822at2; -. DR Proteomes; UP000001683; 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..308 FT /note="Glutaminase" FT /id="PRO_1000132909" FT BINDING 66 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 244 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 308 AA; 33820 MW; AB01FAB6E85734C3 CRC64; MINNVNQEIL RAFVENNRPL AHDGRLPTYI PALMNANKQD FGIHITELDG NSHYYGSFQI PFTVQSISKI ITLAMAIMDN GEELVFSRVG MEPTEDKFNS ILPLEMSSAY PPNPMINAGA IVVTSLIKGR TAGEQFERIL DFTRALADNK NIQVDENAFL SERETGNMNR SLAYYLKDAN VINGNVEEIL ETYFRHCSIL VTAEDLSRIA YIFANDGKDI EGKQLIPAKV CKIVRAIMAM SGFYDESGEF AVRVGIPAKS GVGGGIIGVV PGYMGIGLYG PALNNKGTSI VGFNVLEELT SYLQVGIY //