GLSA_BACTN
ID GLSA_BACTN Reviewed; 321 AA.
AC Q8A4M8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313}; OrderedLocusNames=BT_2571;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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:0000255|HAMAP-Rule:MF_00313};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00313}.
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DR EMBL; AE015928; AAO77678.1; -; Genomic_DNA.
DR RefSeq; NP_811484.1; NC_004663.1.
DR RefSeq; WP_008765205.1; NC_004663.1.
DR AlphaFoldDB; Q8A4M8; -.
DR SMR; Q8A4M8; -.
DR STRING; 226186.BT_2571; -.
DR PaxDb; Q8A4M8; -.
DR PRIDE; Q8A4M8; -.
DR EnsemblBacteria; AAO77678; AAO77678; BT_2571.
DR GeneID; 60923743; -.
DR KEGG; bth:BT_2571; -.
DR PATRIC; fig|226186.12.peg.2623; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_10; -.
DR InParanoid; Q8A4M8; -.
DR OMA; RNPMINS; -.
DR Proteomes; UP000001414; 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; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..321
FT /note="Glutaminase"
FT /id="PRO_0000110596"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 321 AA; 34245 MW; 52BD1D10FF682750 CRC64;
MDKKVTLAQL KEVVQEAYDQ VKTNTGGKNA DYIPYLANVN KDLFGISVCL LNGQTIHVGD
TDYRFGIESV SKVHTAILAL RQYGAKEILD KIGADATGLP FNSIIAILLE NDHPSTPLVN
AGAISACSMV QPIGDSAKKW DAIVENVTDL CGSAPQLIDE LYKSESDTNF NNRSIAWLLK
NYNRIYDDPD MALDLYTRQC SLGVTALQLS VAAGTIANGG VNPVTKKEVF DASLAPKITA
MIAAVGFYEH TGDWMYTSGI PAKTGVGGGV MGVLPGQFGI AAFAPPLDGA GNSVKAQLAI
QYVMNKLGLN VFSDNHLIVV D