ID A0A0Q8UWT8_9MICO Unreviewed; 337 AA.
AC A0A0Q8UWT8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=ASE16_17520 {ECO:0000313|EMBL:KRC47139.1};
OS Leifsonia sp. Root227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC47139.1, ECO:0000313|Proteomes:UP000051819};
RN [1] {ECO:0000313|EMBL:KRC47139.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC47139.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC47139.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC47139.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRC47139.1}.
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DR EMBL; LMIO01000004; KRC47139.1; -; Genomic_DNA.
DR RefSeq; WP_055898083.1; NZ_LMIO01000004.1.
DR AlphaFoldDB; A0A0Q8UWT8; -.
DR STRING; 1736496.ASE16_17520; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000051819; 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:UP000051819}.
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 337 AA; 35160 MW; F031F2E7701C14BA CRC64;
MELDVDGVAE RVSTGTLPGW DDVEALVQKA HERNAGVTSG TVADYIPALA AADPALFGVC
VAEVDGATHG AGDVDHAFSI QSISKAFVYA LVCDELGHEL ALERVGVNNT GLAFNSVMAI
ELNDGHPMNP MVNAGALATT ALVPGQTSEA RWAFIQDGLS RFAGRRLELD AAVYESETET
NQRNQAIARL LQSYGRITAD PAEVVDVYTR QCSLLVTARD LAVMGATLAD GGVNPVTGER
VVSAHVCRDT LSVMAASGLY ERSGEWLFEI GMPGKSGVAG GLVAIAPGKA GIGTFSPPLD
AAGNSVRGQR ATAFLSRSLG LNLFSSDVHH PAEGQDR
//
