ID A0A073J798_9BACT Unreviewed; 313 AA.
AC A0A073J798;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=EH55_02080 {ECO:0000313|EMBL:KEJ93582.1};
OS Synergistes jonesii.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Synergistes.
OX NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ93582.1, ECO:0000313|Proteomes:UP000027665};
RN [1] {ECO:0000313|EMBL:KEJ93582.1, ECO:0000313|Proteomes:UP000027665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=78-1 {ECO:0000313|EMBL:KEJ93582.1,
RC ECO:0000313|Proteomes:UP000027665};
RA Coil D.A., Eisen J.A., Holland-Moritz H.E.;
RT "Draft Genome Sequence of Synergistes jonesii.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KEJ93582.1}.
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DR EMBL; JMKI01000002; KEJ93582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A073J798; -.
DR STRING; 2754.EH55_02080; -.
DR eggNOG; COG2066; Bacteria.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000027665; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027665}.
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 313 AA; 33397 MW; 732A08253A0AF287 CRC64;
MENQSDLLNK QLLNDIGNIA RVTSAEGKVA SYIPELSRMS AELFSLSCQP VDSPMVETGD
CGQFFTMQSM AKIISLAFAI EQFGCENVFR HVGMEASADS FNSLMRIEMT SSKPSNPFMN
AGAIAVCSLI FKAYKEESLK RITDFLKSVI GEENGFDEKV FLSEKRSADR NRALAFFMKS
MGLLHGDVEA ILDLYFTLCS LRCTSGGLAK IGAMIASGGT SVVSGEKLIA NETVYTLLGL
MSSCGLYNES GEFAVRVGLP GKSGVSGGIL AVVPGRMGIG VFSPALNAKG NSVAGIRALE
LLSEKLDLRG LGL
//
