ID A0A368TLZ7_9GAMM Unreviewed; 306 AA.
AC A0A368TLZ7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=DU506_20690 {ECO:0000313|EMBL:RCV85729.1};
OS Halomonas rituensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2282306 {ECO:0000313|EMBL:RCV85729.1, ECO:0000313|Proteomes:UP000253204};
RN [1] {ECO:0000313|EMBL:RCV85729.1, ECO:0000313|Proteomes:UP000253204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TQ8S {ECO:0000313|EMBL:RCV85729.1,
RC ECO:0000313|Proteomes:UP000253204};
RA Lu H., Xing P., Wu Q.;
RT "Halomonas rutogse sp. nov., isolated from Lake TangqianCo on Tibetan
RT Plateau.";
RL Submitted (JUL-2018) 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:RCV85729.1}.
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DR EMBL; QPIJ01000112; RCV85729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368TLZ7; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000253204; 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}.
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 157
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 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 306 AA; 32932 MW; FC0C50CDA18D9855 CRC64;
MQELINDIAA TMAKAEERGK VADYIPELGH VDPQQFGISL ATVDGKVYSA GCATTPFSIQ
SISKVFTLTI ALGQMGDWLW SKVGREPSGD PFNSIVQLEH ESGKPRNPFI NAGAIAVVDA
IMMGHEPKET LGEILNFVRY VANDDSICFD HAVAASEMAH RDRNASLAHF MKAFGHLDHD
VDKVLGIYFH QCAIAMSCEQ LAHAGLFLAS DGINKPSDIR VVAPQRARRI NSLMMMCGHY
DASGEFAFRV GLPGKSGVGG GILAISPSHG SIAVWSPGLD AYGNSLLGTQ ALEMFVQRTG
WSVFGH
//
