ID A0A1G8B5L4_9MICO Unreviewed; 385 AA.
AC A0A1G8B5L4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN04489810_2607 {ECO:0000313|EMBL:SDH28476.1};
OS Microbacterium pygmaeum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=370764 {ECO:0000313|EMBL:SDH28476.1, ECO:0000313|Proteomes:UP000199009};
RN [1] {ECO:0000313|EMBL:SDH28476.1, ECO:0000313|Proteomes:UP000199009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23142 {ECO:0000313|EMBL:SDH28476.1,
RC ECO:0000313|Proteomes:UP000199009};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00313}.
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DR EMBL; LT629692; SDH28476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8B5L4; -.
DR STRING; 370764.SAMN04489810_2607; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000199009; Chromosome i.
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 InterPro; IPR002645; STAS_dom.
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 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:UP000199009}.
FT DOMAIN 308..385
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 385 AA; 40611 MW; 246D861F2D1C5660 CRC64;
MLLEAALDDI RPRTSGAPAG YIPELADADP DRLALAVVGP RGRVITAGDD HVEFTIQSMS
KPFVLALALQ TMGRDSVFGR VGAEPSGEPF NAISLEPGTG RPANPMVNAG AIATTALIAG
EDIDQRTARV IEMMSAFAGR SLWVDEAVYR SKSATGDRNR ALAHLLKSYG HIAGRVDDVV
ESYFRQCSVL VTVRDLAVMA ATLAFGGRNP VTGDRVVDER VARDVTSIMA SCGMYDFSGE
WLLRVGLPAK SGVSGGVLAV APSQFGVAAF SPRLDEHGNS VRASAVVEML SERFGMHLLE
PHESIAEPGV VIEASPGGPI VRLSGELGFA GAERALSLLK EIAASVPDGA EVVVDATALA
RTHPAAITVM RDEFAQLAPR FRLLE
//
