ID GLSA_RALN1 Reviewed; 304 AA. AC Q8XQS6; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 108. 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=RSp1143; ORFNames=RS05469; OS Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum). OG Plasmid megaplasmid Rsp. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000; RX PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M., RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M., RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M., RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P., RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). 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; AL646053; CAD18294.1; -; Genomic_DNA. DR RefSeq; WP_011004432.1; NC_003296.1. DR AlphaFoldDB; Q8XQS6; -. DR SMR; Q8XQS6; -. DR STRING; 267608.RSp1143; -. DR EnsemblBacteria; CAD18294; CAD18294; RSp1143. DR GeneID; 60504053; -. DR KEGG; rso:RSp1143; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_1_4; -. DR Proteomes; UP000001436; Plasmid megaplasmid Rsp. 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; Plasmid. FT CHAIN 1..304 FT /note="Glutaminase" FT /id="PRO_0000110618" FT BINDING 63 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 157 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 240 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 304 AA; 33262 MW; 03B1D8BBF4AC88B9 CRC64; MDYQAILETI HRDIQPWLGK GRVADYIPEL AKASATDFGM AIVTPRGEVF RVGQAETLFS IQSISKLFAC TLAFQLEGES LWQRVGREPS GNAFNSLVQL EHENGIPRNP FINAGALVVT DVLCRRFVQA ETAMVQFMRR LVDNPRVDYN PRVALSELEH ADRNRAMAHF MRSFGNLHMP VETVIDAYCR QCAIEMHCVD LARAVLFLAN GGVVPWSGER VIETSPAKRL SALMLTCGTY DAAGDFVYRV GLPAKSGVGG GIVAVLPGEF GVCVWSPGLD VSGNSLAGLQ ALEWLTTLSG RSIF //