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Database: UniProt
Entry: A0A2A9DNF1_9CORY
LinkDB: A0A2A9DNF1_9CORY
Original site: A0A2A9DNF1_9CORY 
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
//
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