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Database: UniProt
Entry: G0HAH2_CORVD
LinkDB: G0HAH2_CORVD
Original site: G0HAH2_CORVD 
ID   G0HAH2_CORVD            Unreviewed;       420 AA.
AC   G0HAH2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
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:AEK36579.1};
GN   OrderedLocusNames=CVAR_1223 {ECO:0000313|EMBL:AEK36579.1};
OS   Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS   NCIMB 30131) (Corynebacterium mooreparkense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36579.1, ECO:0000313|Proteomes:UP000006659};
RN   [1] {ECO:0000313|EMBL:AEK36579.1, ECO:0000313|Proteomes:UP000006659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC   {ECO:0000313|Proteomes:UP000006659};
RX   PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA   Schroeder J., Maus I., Trost E., Tauch A.;
RT   "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT   from the surface of smear-ripened cheeses and insights into cheese ripening
RT   and flavor generation.";
RL   BMC Genomics 12:545-545(2011).
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}.
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DR   EMBL; CP002917; AEK36579.1; -; Genomic_DNA.
DR   RefSeq; WP_014009765.1; NC_015859.1.
DR   AlphaFoldDB; G0HAH2; -.
DR   STRING; 858619.CVAR_1223; -.
DR   KEGG; cva:CVAR_1223; -.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_0_0_11; -.
DR   Proteomes; UP000006659; Chromosome.
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; 1.
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; PF13466; STAS_2; 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}.
FT   DOMAIN          332..393
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         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   420 AA;  44395 MW;  A1E042B7C0A50AD0 CRC64;
     MEIPLRSYLD DILDDVRPHD DGAVADYIPE LAAADPEPLA VALCTSAGRV YSAGGPHADD
     EREFTIQSIS KPFAYAVALQ EVGVEKVLST VGMEPSGEAF NELSLDGGTH RPVNPMINAG
     AIAVNQLING EDSSVAARVE VLLDYFSRLA GRELRIDERV TGSELATADR NLALAHMLRS
     YGVIGDSAQD AVTGYVRQCS ILVTVKDLAV IGATLALGGR QPVTGEQVLD PRVCRQVQAV
     MASAGMYDGA GKWMAGVGIP AKSGVAGGLM GTLPGQLGIA TFSPRLDASG NSVRGTEIFR
     RMSEDMGLHL MSAVPARGSA VRSIRQRGLG TVIRLQGGLG FAGAEDFLAT VAGHELKTNR
     VVVDMRRVTD VDGFGRAMVL EGLRRIREDG HRIGVIDPDG LLGDRTMDDG TSVETSDEEV
//
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