GLSA_SHESA
ID GLSA_SHESA Reviewed; 304 AA.
AC A0KUF0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Shewana3_1184;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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}.
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DR EMBL; CP000469; ABK47419.1; -; Genomic_DNA.
DR RefSeq; WP_011621971.1; NC_008577.1.
DR AlphaFoldDB; A0KUF0; -.
DR SMR; A0KUF0; -.
DR STRING; 94122.Shewana3_1184; -.
DR EnsemblBacteria; ABK47419; ABK47419; Shewana3_1184.
DR GeneID; 58507527; -.
DR KEGG; shn:Shewana3_1184; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_6; -.
DR OMA; RPRNPFI; -.
DR OrthoDB; 1288854at2; -.
DR Proteomes; UP000002589; 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.
FT CHAIN 1..304
FT /note="Glutaminase"
FT /id="PRO_1000048360"
FT BINDING 63
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 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 189
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; 32925 MW; 40DD255431CEECD4 CRC64;
MPEQALLEEV VDKVRPLLGQ GKVANYIPAL ANVDAGKLGI AVTTIDGETI GAGDYLEPFS
IQSISKVFSL TLALTLYEET EIWSRVGKEP SGHSFNSLVQ VELERGKPRN PFINAGALVI
ADLLQSRLGA PKHRMLELVR ALSQNDKVCF DKQVADSEYQ HSARNAAIAY LMKSFGNFQG
DVDTVLRTYF HYCALKMNCA DLSRAMLYLA NRGKTLDGTE LISQVQTRQL NALLATSGLY
DGAGEFAYRV GMPGKSGVGG GIIAVIPGEL SVCVWSPELD NQGNSLAGTA MLEHLSQRLG
RSIF