GLSA_EXISA
ID GLSA_EXISA Reviewed; 313 AA.
AC C4L2C1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=EAT1b_2251;
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC unclassified Exiguobacterium.
OX NCBI_TaxID=360911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b;
RX PubMed=21460088; DOI=10.1128/jb.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(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: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; CP001615; ACQ71173.1; -; Genomic_DNA.
DR RefSeq; WP_015880732.1; NC_012673.1.
DR AlphaFoldDB; C4L2C1; -.
DR SMR; C4L2C1; -.
DR STRING; 360911.EAT1b_2251; -.
DR EnsemblBacteria; ACQ71173; ACQ71173; EAT1b_2251.
DR KEGG; eat:EAT1b_2251; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_9; -.
DR OMA; RPRNPFI; -.
DR OrthoDB; 1288854at2; -.
DR Proteomes; UP000000716; 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..313
FT /note="Glutaminase"
FT /id="PRO_1000205062"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 313 AA; 34412 MW; 04450E14AA9367DC CRC64;
MNVLEQQLNH LVDECRPYTA QGKVADYIPE LAHVKNDLLG VAICLPDGTY IHAGDVHHKF
TIQSVSKALT LCYVLMEFGE DYVFSKVGME PTGDAFNSIA KLEETVPSKP LNPMINAGAL
AVTSMILGET AELKIYQFRQ FLATLLNRSV EEVTYDEKVA RSEYETTDLN RALLYFMRHH
GIVEGDVDEI IDVYTKQCAI EIDCFDLARI GRVFAGNGED PDTGEELIPR RVVRIVKAIM
TTCGMYDASG EFAVRVGLPG KSGVSGAILA VGNHELDLNN VGFGIFGPAL DSKGNSIAGM
KLLELLIERY TSR