ID A0A2A9DNF1_9CORY Unreviewed; 425 AA.
AC A0A2A9DNF1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=ATK06_1227 {ECO:0000313|EMBL:PFG28134.1};
OS Corynebacterium renale.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1724 {ECO:0000313|EMBL:PFG28134.1, ECO:0000313|Proteomes:UP000221653};
RN [1] {ECO:0000313|EMBL:PFG28134.1, ECO:0000313|Proteomes:UP000221653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20688 {ECO:0000313|EMBL:PFG28134.1,
RC ECO:0000313|Proteomes:UP000221653};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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:PFG28134.1}.
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DR EMBL; PDJF01000001; PFG28134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9DNF1; -.
DR STRING; 1724.GCA_001044175_01753; -.
DR Proteomes; UP000221653; 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 Gene3D; 3.30.750.24; STAS domain; 2.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR002645; STAS_dom.
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; PF04960; Glutaminase; 1.
DR Pfam; PF01740; STAS; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 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:UP000221653}.
FT DOMAIN 319..405
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 425 AA; 46321 MW; 309F70334114A092 CRC64;
MTEHIANPIP AYLRRLLEEV RDQDGGEVAD YIDELAAADP SKLGIALTTV SGHTYSAGDC
DDEFSIQSIS KPFVYALALQ EHGLDAVHEI VGLEPSGEKF NELSLDQDKR PMNPMINAGA
IVVNQLINGP DSTVEDRVDI IVDLFSRLAG RQLRMDADLS YSELKGADRN LSLAHMLRSY
GMISDQAHDA VLSYTMQCSI MVTARDLAAM TATLGNGGVN PLTGEVVLDA EACRLAMSVM
SSSGMYDGAG RWMARVGIPA KSGVAGGLIG TLPGQLGIAT FSPRLDPQGN SVRGLKIFEK
FSEEMGLHLM NPHRMGVHAV RSMQQYDDTM IITLQGTINF SAAEQILYRI SQHDFTASKL
VLDVTRVITV DDISRHFLAS TLLKMRKAGL EISLYDPEDQ LHDLVLSDEY HVPVISAEQR
KAAED
//