ID GLSA_COREF Reviewed; 423 AA.
AC Q8FMX4;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Glutaminase;
DE EC=3.5.1.2;
GN Name=glsA; OrderedLocusNames=CE2375;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR EMBL; BA000035; BAC19185.1; -; Genomic_DNA.
DR RefSeq; WP_006768381.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FMX4; -.
DR SMR; Q8FMX4; -.
DR STRING; 196164.gene:10742812; -.
DR KEGG; cef:CE2375; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_0_0_11; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000001409; 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; 2.
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 SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..423
FT /note="Glutaminase"
FT /id="PRO_0000110605"
FT DOMAIN 321..423
FT /note="STAS"
FT REGION 27..312
FT /note="Glutaminase"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 45863 MW; CDEB65C617F289CB CRC64;
MTTHPLTMPI PEYFEEILES VRSDVSGEVA QYIPQLKDAD PNPLALAMCT VDGHIYGAGD
DEHEFTMQSV SKPFAYALAL QEQGPEKVFA TVGLEPSGEA FNELSLDGST NRPMNPMINA
GAIAVNQLIN GSESSVEDRV EKIRSYFSAL AGRELNIDRQ LSETEIEGAD RNLSIAHMLR
NYGIIEDDAH DAVLSYTLQC SVKVTARDLA VMTATLAAGG TQPLTGEKLV DARVARLVLS
TMASAGMYDE AGQWLATVGI PAKSGVSGGL VGVLPGQLGL ATFSPRLNSQ GNPVRGVEIF
KALSEDMGLH LMSAELLTQH AVRAIEERGD TTVIQLQGAM NFSAAENFLF TVTDHDFTGE
KVVLDISRVP MFRPMGRRLV KEGLRRIRDN GFKVAIYDPE DILPDFDFSD GTKSPQVDDP
EEL
//
