ID A0A2A3AGC9_9MICC Unreviewed; 613 AA.
AC A0A2A3AGC9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ECO:0000313|EMBL:PBB08419.1};
GN ORFNames=CKW39_08615 {ECO:0000313|EMBL:PBB08419.1};
OS Kocuria sp. WRN011.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=2029858 {ECO:0000313|EMBL:PBB08419.1, ECO:0000313|Proteomes:UP000218573};
RN [1] {ECO:0000313|EMBL:PBB08419.1, ECO:0000313|Proteomes:UP000218573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRN011 {ECO:0000313|EMBL:PBB08419.1,
RC ECO:0000313|Proteomes:UP000218573};
RA Zhang G., Wu G.;
RT "Kocuria alkalisoli sp. nov., isolated from saline alkaline soil.";
RL Submitted (AUG-2017) 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:PBB08419.1}.
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DR EMBL; NSGI01000005; PBB08419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3AGC9; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000218573; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 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:UP000218573}.
FT DOMAIN 473..575
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 250
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"
SQ SEQUENCE 613 AA; 67204 MW; C488507DC26E2683 CRC64;
MSTVPKTKLG PSVITEYLQR VVEDLREVEG GAVKDSIPAL ANADPHPIGI AVATVDGAIY
QAGDSKQEFC IQSISKAFTY AQALTDRGMD GVFEKIDVEP SGDAFNEISL QPETGRPANP
MINAGAIAAT SLVKNTAHGT RRERILRLYS RLAGRQLRIN KTIHAQEHRS GDRNRALGWL
LSSRDIIEGD PTDALEDYFA QCSVMLNCVD LARMGATLAA GGVNPLSGER VLDTQVVSDV
LSVMYTCGMY DDAGRWALKV GLPAKSGVAG GIIAVLPGQL AVAVFSPPLD QHGNSVRGVA
ACERLTQDLD LHFARTERNG HSTVRSEYYL SEAPSLMRRN DAANEVLEEH GEDVRIVELQ
GDLRFAGAET AIRTIREAAR ECTYVLVDIR QVDDLARYVM PLLGRTSEQL ENAQRHLAII
AEKGSEHTQD LDHPVTVFPT RAEALTWAED RILEKFGGPE CMPDKVHSTD SDLLSSLSDD
DVAEIRSKTT RVEWPAGTTV LRAGQRFEGV YMVVSGNVEI TRRSPTGERV ELEVLGPGKS
FGEVALGTDS RHMVSFTTLT DVIARKLPPE AVDEIEKTHP ELALRWWRAV STHAMRRIEE
RWRQQAGETH TAD
//
