ID D0I4Q8_GRIHO Unreviewed; 306 AA.
AC D0I4Q8;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Glutaminase {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
GN Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN ORFNames=VHA_000723 {ECO:0000313|EMBL:EEY73475.1};
OS Grimontia hollisae CIP 101886.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Grimontia.
OX NCBI_TaxID=675812 {ECO:0000313|EMBL:EEY73475.1, ECO:0000313|Proteomes:UP000003604};
RN [1] {ECO:0000313|EMBL:EEY73475.1, ECO:0000313|Proteomes:UP000003604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 101886 {ECO:0000313|EMBL:EEY73475.1,
RC ECO:0000313|Proteomes:UP000003604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Saunders E.H., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (OCT-2009) 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:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC Rule:MF_00313};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076, ECO:0000256|HAMAP-Rule:MF_00313}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEY73475.1}.
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DR EMBL; ADAQ01000009; EEY73475.1; -; Genomic_DNA.
DR RefSeq; WP_005502004.1; NZ_ADAQ01000009.1.
DR AlphaFoldDB; D0I4Q8; -.
DR GeneID; 58895673; -.
DR eggNOG; COG2066; Bacteria.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000003604; Unassembled WGS sequence.
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 Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00313};
KW Reference proteome {ECO:0000313|Proteomes:UP000003604}.
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 306 AA; 33304 MW; 4025865863297CC6 CRC64;
MKPTPALLSR ILEEVRPLIG QGKVADYIPA LKKVPASKLG IAVCYNDGEI IKAGDAEEAF
SIQSISKVLS LTLALQNYQP EEIWRRVGKE PSGQAFNSMI QLEMEQGIPR NPFINAGALV
VCDMLHSRLS APRQRMLEFV RRLSGNEHIC YDKVVAMSEM DHSDRNAAIA YLMRSFGNFE
NEVMPVLANY FHYCALRMSC VDLAKTFNYL ANKGLPLGAE KTIVSQTQCK QVNALLATCG
LYDGAGEFAY RVGMPGKSGV GGGIIAIVPG EMSIAVWSPE LDPSGNSLAG TAALELLAER
IGRSIF
//