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Database: UniProt/TrEMBL
Entry: B2GG47_KOCRD
LinkDB: B2GG47_KOCRD
Original site: B2GG47_KOCRD 
ID   B2GG47_KOCRD            Unreviewed;       613 AA.
AC   B2GG47;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
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:BAG30248.1};
GN   OrderedLocusNames=KRH_19010 {ECO:0000313|EMBL:BAG30248.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30248.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30248.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG30248.1; -; Genomic_DNA.
DR   RefSeq; WP_012398969.1; NC_010617.1.
DR   AlphaFoldDB; B2GG47; -.
DR   SMR; B2GG47; -.
DR   STRING; 378753.KRH_19010; -.
DR   KEGG; krh:KRH_19010; -.
DR   eggNOG; COG0664; Bacteria.
DR   eggNOG; COG1366; Bacteria.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_3_1_11; -.
DR   OrthoDB; 9788822at2; -.
DR   Proteomes; UP000008838; Chromosome.
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; 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; 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.
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:UP000008838}.
FT   DOMAIN          352..421
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
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;  66765 MW;  8E4FF2F92EB88D44 CRC64;
     MSTVPMSKLG PSPVTEYLRR VVEDLRSVEG GAVNTSIPEL ANADPATVGI AVATVDGALY
     QAGDTRHEFC LQSISKAFTY AQALTDRGAD GVFEKIDVEP SGDAFNEISL QPETGRPSNS
     MINAGAIAAT SLVRNTSHGT RMERILRLYS ACAGRRLRIN KNVQAQERRA GDRNRALGWL
     LTSRGIIDGD PTGALDDYFG QCAVMLNCVD LARMGATLAA GGRNPVTGER VLEPEVVSDV
     LSVMSTCGMY DDAGRWALRV GLPAKSGVSG GVIAVLPGQL AVAVFSPPLD RHGNSVRGVA
     ACERLTQDLD LHFARTERNG HSTVRSEYTL AEAPSLVRRN EAASEVLEQH GEDARIIELQ
     GDLRFAGAET AVRTVRDAAR RSRYVLVDIR QVDDMARFVI PMLSRTAEQV ESTGHHMVLI
     AEKSGEHTRG LEHPMTVFAT RAEALTWAEE RILEQFGDAT CTPDNVHSTR SELLSTLAEE
     DVRRIRAHTE SVEWDAGATL LRTGQKFSGV YMVTSGSVEV SRRSPQGDRV ELEVIGPGMS
     FGEIALGTEL RYLVTFTALT PVTAHRLSPE AIARIEEEDP ALALRWWRAV SQQAMLRIEE
     RWRQQAGETH TAD
//
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