ID B6VNH5_PHOAA Unreviewed; 317 AA.
AC B6VNH5; C7BIK2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
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 OrderedLocusNames=PAU_03288 {ECO:0000313|EMBL:CAQ85376.1};
GN ORFNames=PA-RVA20-21-0092 {ECO:0000313|EMBL:CAR67705.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAR67705.1};
RN [1] {ECO:0000313|EMBL:CAR67705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43949 {ECO:0000313|EMBL:CAR67705.1};
RX PubMed=18838673; DOI=10.1073/pnas.0711114105;
RA Waterfield N.R., Sanchez-Contreras M., Eleftherianos I., Dowling A.,
RA Wilkinson P., Parkhill J., Thomson N., Reynolds S.E., Bode H.B., Dorus S.,
RA Ffrench-Constant R.H.;
RT "Rapid virulence annotation (RVA): identification of virulence factors
RT using a bacterial genome library and multiple invertebrate hosts.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15967-15972(2008).
RN [2] {ECO:0000313|EMBL:CAQ85376.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC43949 {ECO:0000313|EMBL:CAQ85376.1};
RA Crossman L.C.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAR67705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43949 {ECO:0000313|EMBL:CAR67705.1};
RA Thomson N.R.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CAQ85376.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747}, and
RC ATCC43949 {ECO:0000313|EMBL:CAQ85376.1};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM162591; CAQ85376.1; -; Genomic_DNA.
DR EMBL; FM211060; CAR67705.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VNH5; -.
DR STRING; 291112.PAU_03288; -.
DR KEGG; pay:PAU_03288; -.
DR eggNOG; COG2066; Bacteria.
DR Proteomes; UP000002747; 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; 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 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 317 AA; 34629 MW; AF7A58BB2500CB74 CRC64;
MPLSGVKSVS STTFSNTLLS DILRQIRPLI GQGKVANYIP ALAEVPADNL AIAICTIDGQ
IFHAGDAEKR FSIQSISKIF SLTLAMTRYQ EQEIWQRVGQ EPSGQPFNSL VQLELEKGKP
RNPFINAGAL VVCDMLQSRL SAPKQRMLEV VRKLAGCSDI CYDNKVARSE MEHSHRNAAI
AYLMKSFGNF DNDVLAVLQT YFHYCALKMN CIELARCFVY LANQGSTIGA EQQILSPRQT
RQINALMMTC GMYDGSGEFA FRIGMPGKSG VGGGIVCVVP GEFTVAVWSP ELDRSGNSLA
GCAALELLAD RIGRSVF
//