GLSA_SHEPC
ID GLSA_SHEPC Reviewed; 304 AA.
AC A4Y8Y3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Sputcn32_2697;
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 / ATCC BAA-453;
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., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-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; CP000681; ABP76416.1; -; Genomic_DNA.
DR RefSeq; WP_011788663.1; NC_009438.1.
DR AlphaFoldDB; A4Y8Y3; -.
DR SMR; A4Y8Y3; -.
DR STRING; 319224.Sputcn32_2697; -.
DR GeneID; 45043174; -.
DR KEGG; spc:Sputcn32_2697; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_6; -.
DR OMA; RPRNPFI; -.
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_1000048359"
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; 32911 MW; D9C219EE77DEC89B CRC64;
MPELALLEEV VEKVRPLLGQ GKVANYIPAL ASVDAGKLGI AVTTVDGETL GAGDYLEPFS
IQSISKVFSL TLALTLYEEA EIWSRVGKEP SGHSFNSLVQ VELERGKPRN PFINAGALVI
ADLLQSRLGA PKHRMLELVR QLSQNDKVCF DKQVADSEYQ HSARNAAIAY LMKSFGNFQG
DVDTVLRTYF HYCALKMNCA DLSRAMLYLA NRGKTVDGTE LISQVQTRQL NALLATSGLY
DGAGEFAYRV GMPGKSGVGG GIIAVIPGEL SICVWSPELD ENGNSLAGTA MLEHLSQRLG
RSIF