GenomeNet

Database: UniProt
Entry: B6VNH5_PHOAA
LinkDB: B6VNH5_PHOAA
Original site: B6VNH5_PHOAA 
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
//
DBGET integrated database retrieval system