ID G7EMN0_9GAMM Unreviewed; 307 AA.
AC G7EMN0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ECO:0000313|EMBL:GAA62153.1};
GN ORFNames=P20652_4049 {ECO:0000313|EMBL:GAA62153.1};
OS Pseudoalteromonas sp. BSi20652.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=388384 {ECO:0000313|EMBL:GAA62153.1, ECO:0000313|Proteomes:UP000005499};
RN [1] {ECO:0000313|Proteomes:UP000005499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bsi20652 {ECO:0000313|Proteomes:UP000005499};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(2012).
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:GAA62153.1}.
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DR EMBL; BADT01000250; GAA62153.1; -; Genomic_DNA.
DR RefSeq; WP_008172944.1; NZ_BADT01000250.1.
DR AlphaFoldDB; G7EMN0; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000005499; 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}.
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 307 AA; 33767 MW; DCF7AEA36F1A90D0 CRC64;
MPTADYQKVL DEIVHEVRPL LSQGKVADYI PALAEVDPEQ FSIAIYTTDG ETVCAGDCSQ
RFTIQSVSKV MTLTMALQRY GDELWHRVGK EPSGTAFNSL TQLEFEKGIP RNPFINAGAI
VTCDALYSRL SAPMHSMLET FRLLAGNRGI IIDKKVANSE YEFRHRNAAM AHLMKSFGNF
ENEVDDVLWA YFNFCSIELN CIELAKAYNF LANKGVDNRS GNRVLSSRQN KQLNSLLFTS
GLYDAAGDFG YRVGMPGKSG VSGTILAVLP NKFTVAVYSP GLNSFGNSVA GIAALELLSK
KLDISIF
//
