GLSA_SINFN
ID GLSA_SINFN Reviewed; 315 AA.
AC C3MD81;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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}; OrderedLocusNames=NGR_c16350;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(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}.
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DR EMBL; CP001389; ACP25400.1; -; Genomic_DNA.
DR RefSeq; WP_012708169.1; NC_012587.1.
DR RefSeq; YP_002826153.1; NC_012587.1.
DR AlphaFoldDB; C3MD81; -.
DR SMR; C3MD81; -.
DR STRING; 394.NGR_c16350; -.
DR EnsemblBacteria; ACP25400; ACP25400; NGR_c16350.
DR KEGG; rhi:NGR_c16350; -.
DR PATRIC; fig|394.7.peg.4451; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_5; -.
DR OMA; RPRNPFI; -.
DR OrthoDB; 1288854at2; -.
DR Proteomes; UP000001054; 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; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..315
FT /note="Glutaminase"
FT /id="PRO_1000132910"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 120
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 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 315 AA; 33838 MW; 7C0303E270407796 CRC64;
MPEQKAPQDL QLILDDIYRE LTPRLGEGKV ADYIPQLARV NPQHFGMAIV TTGGEVHRVG
DAEVPFSIQS ISKVFTLTLA LGKHGENIWH RVGREPSGSA FNSIVQLEHE GGKPRNPFIN
AGAITISDLI LAGHTPKELI GEIVRFVRYL ADDENIVIDH EVARSETVTG FRNFALASFM
RSFGRLDHPV EHVLGVYFHH CALAMTCSQL AKAGLFLAAG GTNPLTGHSV VSRQRARRIN
ALMLTCGHYD GSGDFAYRVG LPGKSGVGGG IMAVAPGKAS IAVWSPGLNE NGNSLLGSLA
LEMLAARTGW SVFGP