GLSA_PSEU2
ID GLSA_PSEU2 Reviewed; 302 AA.
AC Q4ZU37;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Psyr_2292;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY37335.1; -; Genomic_DNA.
DR RefSeq; WP_011267568.1; NC_007005.1.
DR RefSeq; YP_235373.1; NC_007005.1.
DR AlphaFoldDB; Q4ZU37; -.
DR SMR; Q4ZU37; -.
DR STRING; 205918.Psyr_2292; -.
DR EnsemblBacteria; AAY37335; AAY37335; Psyr_2292.
DR KEGG; psb:Psyr_2292; -.
DR PATRIC; fig|205918.7.peg.2344; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_6; -.
DR OMA; RPRNPFI; -.
DR Proteomes; UP000000426; 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; -; 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..302
FT /note="Glutaminase"
FT /id="PRO_1000048346"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 302 AA; 32683 MW; 3B89044D56115EFC CRC64;
MQDLLNEILD EVRPLLGQGK VADYIPALGE VRPDQLGIAV YGNDGQVFSA GDAETAFSIQ
SISKVFSLVQ AINHSGEEIW QRLGHEPSGQ PFNSLVQLEF EQGRPRNPFI NAGALVICDI
NQARFAAPSL SMRDFVRRLC GNRAITSDSK VADSEYQHRS RNAAAAYLMK SFDNFHGDVE
DVLRSYFHHC ALSMNCIDLA KAFGFLAHQG FCAHSGEQVL TARQATQVNS IMATSGLYDE
AGNFAYRVGL PGKSGVGGGI VAIVPERASV CVWSPELNAA GNSLVGMAAL EKLSARVDWS
VF