ID A0A3L7E439_9GAMM Unreviewed; 338 AA.
AC A0A3L7E439;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=DWB85_01700 {ECO:0000313|EMBL:RLQ23293.1};
OS Seongchinamella sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Seongchinamella.
OX NCBI_TaxID=2283635 {ECO:0000313|EMBL:RLQ23293.1, ECO:0000313|Proteomes:UP000265509};
RN [1] {ECO:0000313|EMBL:RLQ23293.1, ECO:0000313|Proteomes:UP000265509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0301 {ECO:0000313|EMBL:RLQ23293.1,
RC ECO:0000313|Proteomes:UP000265509};
RA Ye M.-Q., Du Z.-J.;
RT "Halioglobus sp. genome submission.";
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|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:RLQ23293.1}.
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DR EMBL; QRAN01000002; RLQ23293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7E439; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000265509; 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:SF48; GLUTAMINASE 1; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..338
FT /note="Glutaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017963968"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 338 AA; 36339 MW; 5602BD0DE9D07E00 CRC64;
MLLRPLKYTL ALALLAVSAS SLAATITAQD YQRVVKEAYA KFKDVREGAN ADYIPILATV
PSEMFGVAII TRDGEVYSAG ELDYEFSIQS VSKPFTASLI MQQQGPKTLR EKIGVEPTGL
PFNSKIALEI YEERSVNPLV NAGAIAAVSL VEADSEKARW QQVLGNIEAY AGRDLEVLEE
VYDSEYETAW GNRAIANLLF NYGRLYSEPE QALRVYTRQC SIGINTLDLA MMGATLANEG
VNPKTGKRVL DKAHVPELLA IMATAGFYDE SGEWMYRAGL PAKTGVGGGI VAVVPGKFAI
ATFSPPLNPA GNSVRGLKAI SYIAAELGVG LYGPNAGE
//
