ID E4KWV2_9FIRM Unreviewed; 307 AA.
AC E4KWV2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
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_2 {ECO:0000313|EMBL:EFR33671.1};
GN Synonyms=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN ORFNames=HMPREF9286_1632 {ECO:0000313|EMBL:EFR33671.1};
OS Peptoniphilus harei ACS-146-V-Sch2b.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR33671.1, ECO:0000313|Proteomes:UP000003705};
RN [1] {ECO:0000313|EMBL:EFR33671.1, ECO:0000313|Proteomes:UP000003705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR33671.1,
RC ECO:0000313|Proteomes:UP000003705};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFR33671.1}.
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DR EMBL; AENP01000004; EFR33671.1; -; Genomic_DNA.
DR RefSeq; WP_005955224.1; NZ_AENP01000004.1.
DR AlphaFoldDB; E4KWV2; -.
DR eggNOG; COG2066; Bacteria.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000003705; 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:UP000003705}.
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 166
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 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 307 AA; 33844 MW; BEAE36E6B50BA6C8 CRC64;
MIYSEEVLGK ALNLGRKYIH EGAVADYIPE LAKVDANKLA ISTIEDGNIY SVGDSKVRYS
IQSIVKVILY ALAMENYKVS ELKKYVGVRP SAKPFNSVIE LELSEKKIPV NPFINAGAII
IVAILYNVYR EKTFDVILEK ASQFLGEDVD YSREIAQSEK ESSFTNRTLI YLMLAKGILP
SDTKVEEVLD TYFKACSILV NTENLAHMSY VISNNGLDIE GKKVISPNEA RVLRSLMATC
GTYDYSGDFA IRVGLPAKSG VGGGIVTASN NKTGLAVYAP RLDTHGNSYS GVRMLEYLSQ
ELDLSIY
//
