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Database: UniProt
Entry: A0A172U3Z6_9BACT
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ID   A0A172U3Z6_9BACT        Unreviewed;       330 AA.
AC   A0A172U3Z6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=SY85_24555 {ECO:0000313|EMBL:ANE53707.1};
OS   Flavisolibacter tropicus.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE53707.1, ECO:0000313|Proteomes:UP000077177};
RN   [1] {ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANE53707.1, ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|EMBL:ANE53707.1,
RC   ECO:0000313|Proteomes:UP000077177};
RX   PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA   Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA   Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT   "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL   Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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|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; CP011390; ANE53707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A172U3Z6; -.
DR   STRING; 1492898.SY85_24555; -.
DR   KEGG; fla:SY85_24555; -.
DR   PATRIC; fig|1492898.3.peg.5335; -.
DR   Proteomes; UP000077177; 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   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF48; GLUTAMINASE 1; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 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:UP000077177}.
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   330 AA;  35110 MW;  2E9059CA379C4E6D CRC64;
     MVRAQAKTQA PKAATTGSLS DADIEAALTE AYNKFKDLKE GKNADYIKEL ANVDPNIFGI
     VLITTDGRVF TKGDITSMVS IQSVSKVFTM AKVLEEQGHQ AVMDKIGVDA TGMRFNSIVA
     VELQRGKEIN PLVNPGAIAA SSLIGGADSA AKWKNIMDIH NQFAGRQLSV NWPVYVSEAG
     DNLRNQAIAH LLKAYNRMYF DPVQATDIYT KQCAINVNAK DLATMAATLA NGGVNPVTKK
     KVVSPETVMY TLPVMATAGL YDDSGIWLYN SGLPAKSGVG GGLLAVCPGK FGIAAVSPPL
     DAAGNSVKSQ KAINYVVEKL KADPYLVQPK
//
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