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Database: UniProt
Entry: F3GGG5_PSESJ
LinkDB: F3GGG5_PSESJ
Original site: F3GGG5_PSESJ 
ID   F3GGG5_PSESJ            Unreviewed;        87 AA.
AC   F3GGG5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
DE   Flags: Fragment;
GN   ORFNames=PSYPI_29204 {ECO:0000313|EMBL:EGH46165.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH46165.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH46165.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH46165.1,
RC   ECO:0000313|Proteomes:UP000004986};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
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};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
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:EGH46165.1}.
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DR   EMBL; AEAI01001513; EGH46165.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3GGG5; -.
DR   PATRIC; fig|629263.4.peg.4707; -.
DR   HOGENOM; CLU_173833_0_0_6; -.
DR   BioCyc; PSYR629263:G11X0-5317-MONOMER; -.
DR   Proteomes; UP000004986; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGH46165.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGH46165.1"
SQ   SEQUENCE   87 AA;  9147 MW;  D86A68EE36512049 CRC64;
     KYAWPMTRQA TQVNSIMATS GLYDEAGNFA YRVGLPGKSG VGGGIVAIVP ERASVCVWSP
     ELNAAGNSLV GMAALEKLSA RVDWSVF
//
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