ID GLSA_PSEPF Reviewed; 302 AA. AC Q3KAU3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, 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=Pfl01_3373; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). 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; CP000094; ABA75111.1; -; Genomic_DNA. DR RefSeq; WP_011334745.1; NC_007492.2. DR AlphaFoldDB; Q3KAU3; -. DR SMR; Q3KAU3; -. DR KEGG; pfo:Pfl01_3373; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_1_6; -. DR Proteomes; UP000002704; 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. FT CHAIN 1..302 FT /note="Glutaminase" FT /id="PRO_1000048345" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 155 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 186 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 238 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 256 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 302 AA; 32732 MW; EB2A4B2DE6A33BC7 CRC64; MQALLNEILD AVRPLIGQGK VADYIPALGT VPANQLGIAV YGNDGEMYCA GDAETPFSVQ SISKVFSLVQ AIEHSGEAIW ERLGHEPSGQ PFNSLVQLEF ERGRPRNPFI NAGALVICDI NQSRFAAPAL SMRDFVRRLS GNPQVMVDGK VADSEYQHRA RNAAMAYLMQ SFGNFHNDVE AVLRSYFSHC ALRMNCIDLA RAFCFLANDG FCKHSGEQIL TRRQTQQVNS IMATSGLYDE AGNFAYRVGL PGKSGVGGGI VAVVPGQFTV CVWSPELNTA GNSLAGMAAL EMLSSRIGWS VF //