ID GLSA_RHOPB Reviewed; 309 AA. AC Q218T3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 92. 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=RPC_1541; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=316056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., RA Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) 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; CP000301; ABD87103.1; -; Genomic_DNA. DR AlphaFoldDB; Q218T3; -. DR SMR; Q218T3; -. DR STRING; 316056.RPC_1541; -. DR KEGG; rpc:RPC_1541; -. DR eggNOG; COG2066; Bacteria. DR HOGENOM; CLU_027932_1_1_5; -. DR OrthoDB; 9788822at2; -. 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..309 FT /note="Glutaminase" FT /id="PRO_0000336038" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 160 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 167 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" FT BINDING 261 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313" SQ SEQUENCE 309 AA; 32612 MW; F952E6DF53E411DA CRC64; MTELDVVVQE IAEEIAARSD RGSVAHYIPE LAKVDPAGFG LVVIDADGHV AAGGDADTAF SIQSISKVFT LTLALGKIGD RLWQRVGREP SGSPFNSIVQ LEFERGIPRN PFINAGAIAV TDVILSGHQP REALGEILRF MRFLTGDPTI AIDQAVAASE QRTGFRNAAL ANYMKSFGVL DNPVDYTLGV YFHHCAIAMS CRQLALAGRY LAHSGRNPST GHSVVSPGRA RRINAVMLTC GHYDGSGEFA YRVGLPGKSG VGGGVLAIAP GKASIAAWSP GLDASGNSHL GRVALEALSK RMGWSIFGV //