ID A0A2T6BQF8_9BACL Unreviewed; 303 AA.
AC A0A2T6BQF8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=C8P63_11778 {ECO:0000313|EMBL:PTX58330.1};
OS Melghirimyces profundicolus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Melghirimyces.
OX NCBI_TaxID=1242148 {ECO:0000313|EMBL:PTX58330.1, ECO:0000313|Proteomes:UP000244240};
RN [1] {ECO:0000313|EMBL:PTX58330.1, ECO:0000313|Proteomes:UP000244240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45787 {ECO:0000313|EMBL:PTX58330.1,
RC ECO:0000313|Proteomes:UP000244240};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-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:PTX58330.1}.
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DR EMBL; QBKR01000017; PTX58330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6BQF8; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000244240; 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:UP000244240}.
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 165
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 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 303 AA; 33256 MW; 193A3908B689B9E9 CRC64;
MQSFLKELVE KHRPFTREGK LADYIPQLAK QNPSALGVSV RTCEGGVYSA GDCPIEFTLQ
SISKVITLIL ALMDRGEEEV FDHVGMEPTG NPFNSIYDLE VNSPGKPLNP MINAGALVVS
SLIEGSTVEE RLERILTLVR DMAENPDIGV DEAVYHSERV TGYRNRSMAY FLKEFGIVDD
VESTLELYFK HCSISVTCDD LARMGLCLAR YGEDEKGRQV VPRPIARLVK TFMVTCGMYN
ASGEFAIKVG IPAKSGVSGG ILASVPERMG IGVFGPALDE KGNSHAGVRL LKDLSREWNL
SIF
//
