GLSA_SHEB9
ID GLSA_SHEB9 Reviewed; 304 AA.
AC A9KXQ3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Sbal195_3193;
OS Shewanella baltica (strain OS195).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) 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; CP000891; ABX50355.1; -; Genomic_DNA.
DR RefSeq; WP_006085711.1; NC_009997.1.
DR AlphaFoldDB; A9KXQ3; -.
DR SMR; A9KXQ3; -.
DR EnsemblBacteria; ABX50355; ABX50355; Sbal195_3193.
DR GeneID; 11774897; -.
DR KEGG; sbn:Sbal195_3193; -.
DR HOGENOM; CLU_027932_1_1_6; -.
DR OMA; RPRNPFI; -.
DR Proteomes; UP000000770; 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_1000079079"
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; 32782 MW; D3F89341F113E7A3 CRC64;
MPELALLEEV VEKVRPLLGQ GKVADYIPAL ASVDAGKLGI AVTTVDGETL GAGDYLEPFS
IQSISKVFSL TLALTLYEEA EIWSRVGKEP SGHSFNSLVQ VELERGKPRN PFINAGALVI
ADLLQSRLGA PKHRMLELVR QLSQNDKVSF DKQVADSEYQ HSARNAAIAY LMKSFGNFQG
DVDTVLRTYF HYCALKMNCA DLSKAMLYLA NRGKSITGTE LISQVQTRQL NALLATSGLY
DGAGEFAYRV GMPGKSGVGG GIIAVIPGEL SICVWSPELD GNGNSLAGTA MLEHLSQRLG
RSIF