ID GLSA_PHOPR Reviewed; 306 AA. AC Q6LML1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 100. 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=PBPRA3151; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=298386; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). 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; CR378673; CAG21466.1; -; Genomic_DNA. DR RefSeq; WP_011219721.1; NC_006370.1. DR AlphaFoldDB; Q6LML1; -. DR SMR; Q6LML1; -. DR STRING; 298386.PBPRA3151; -. DR KEGG; ppr:PBPRA3151; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_1_6; -. DR Proteomes; UP000000593; Chromosome 1. 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..306 FT /note="Glutaminase" FT /id="PRO_1000048339" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 166 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 242 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 306 AA; 33101 MW; 6BF7AD30710013D4 CRC64; MKPTKELLAG ILDEVRPLIG QGKVADYIPA LAGISATKLG IAVCYNDGEI IQAGDTQERF SIQSISKVMS LTLAMSLYEP EEIWRRVGKE PSGHAFNSMI QLELENGIPR NPFINAGALV VSDLLHSRLA APQYRMLELV RKLSCNPHLT YDKAVAASEM QHSDRNASIA YLMRSFGNFE NEVMPVLTNY FSYCSLNMSC IDLARTFSYL ANKGLPLGAK KTIISQTQSK QMNALLATCG LYDGAGEFAY RVGMPGKSGV GGGIVAIVPG EMSITVWSPE LDPSGNSLAG TAALELLAER IGRSIF //