ID A0A147ERC0_9MICO Unreviewed; 336 AA.
AC A0A147ERC0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=NS354_01945 {ECO:0000313|EMBL:KTR87078.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR87078.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR87078.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR87078.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR87078.1}.
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DR EMBL; LDRK01000010; KTR87078.1; -; Genomic_DNA.
DR RefSeq; WP_058592929.1; NZ_LDRK01000010.1.
DR AlphaFoldDB; A0A147ERC0; -.
DR PATRIC; fig|1079994.3.peg.85; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000070810; 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 Reference proteome {ECO:0000313|Proteomes:UP000070810}.
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 178
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 209
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"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 336 AA; 35474 MW; 8B6FE675A75783AD CRC64;
MFEVDMEGVR QRASTGSLPG RERVAELLRE AHERYAPMRD GVVADYIPVL ARADPDRFGL
SLIGVDGATS EVGAAGDPFT IQSISKAFVF ALVCEAIGHH AVHERVGVNN TGLPFNSVMA
LELNLGSPMN PMVNAGAIAT TAMMPAESHD ERWEAIRGGL SRFAGRELAV DVEVYESEMR
TNTRNRAIAR LLEGYGRLER DPAAIVDMYT RQCALTVTAH DLAVMGATLA DGGVNPVTGV
RVVAEEVARD TLTVLASCGM YERSGEWLFE IGLPAKSGVS GGIVAISPGK GALGSFSPPL
DPAGNSVRGQ RACAFLSRAL GLNLFASGVS RTGSTA
//
