ID GLSA_BORA1 Reviewed; 312 AA. AC Q2KVV8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 94. 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=BAV2794; OS Bordetella avium (strain 197N). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=197N; RX PubMed=16885469; DOI=10.1128/jb.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., RA Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals RT extensive diversity in surface structures associated with host RT interaction."; RL J. Bacteriol. 188:6002-6015(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; AM167904; CAJ50405.1; -; Genomic_DNA. DR RefSeq; WP_012418436.1; NC_010645.1. DR AlphaFoldDB; Q2KVV8; -. DR SMR; Q2KVV8; -. DR STRING; 360910.BAV2794; -. DR GeneID; 41394631; -. DR KEGG; bav:BAV2794; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_0_4; -. DR OrthoDB; 9788822at2; -. DR Proteomes; UP000001977; 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:SF48; GLUTAMINASE 1; 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..312 FT /note="Glutaminase" FT /id="PRO_1000048326" FT BINDING 67 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 118 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 312 AA; 32672 MW; 27E6340D682716DA CRC64; MKIDVSRLSA AVNDAHARHA QAPGGANASY IPYLAKVPSH LAGVAAVTVD GDQVVAGDAD YAFAIESISK VCSLVQALED HGPDAVREKI GADPTGLPFN SVMALALHDG KPLSPLVNAG AIATVSFLKA ANAEERWKKI LAMQSALAGA DIALSDEVNQ SEQTTNFHNR AIAWLLYSAS TMYSDPMEAC EVYTRQCSTL FTARHLATMA ATLAAKGRNP LTGKQVLKPE HVPSVLAEMM MEGLYERSGD WAYMVGLPGK SGVGGGIMAV VPGVMGLAAF SPPLDPAGNS VRGQLMVADV ARTLGLNLFD RA //