ID A0A0M2H1N7_9MICO Unreviewed; 390 AA.
AC A0A0M2H1N7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=glsA1 {ECO:0000313|EMBL:KJL37988.1};
GN Synonyms=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN ORFNames=RS81_02984 {ECO:0000313|EMBL:KJL37988.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL37988.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL37988.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL37988.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL37988.1}.
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DR EMBL; JYIZ01000056; KJL37988.1; -; Genomic_DNA.
DR RefSeq; WP_045276892.1; NZ_JYIZ01000056.1.
DR AlphaFoldDB; A0A0M2H1N7; -.
DR STRING; 92835.RS81_02984; -.
DR PATRIC; fig|92835.4.peg.3013; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
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:SF29; GLUTAMINASE; 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:UP000033956}.
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 390 AA; 41024 MW; 6099618F93822EE0 CRC64;
MEPITALLDE ILEESRALRD GAPADYIPEL AVADPDQLAL AVVGPHGRVR AVGDADAQFT
IQSISKPFVL ALALQERGRE AVLAKVGVEP SGEPFNAISL EAGTGRPANP MVNAGAIATS
ALVVGDEIDD RMTRIVDTLS AFAGRSLWVD EAVYASESAT GDRNRALAHL LRSHGVIDGP
VDIAVETYFR QCSLLVTVRD LAVMAATLAF GGVNPMTGDR VVREEVARDV MSIMASCGMY
DFSGEWLLRV GLPAKSGVSG GLVAVAPSQF GVGAFSPNLD GHGNSVRASS VVEAIAERFG
MHMLEPHESV AVPSIRVQSD ADGRVVRLSG ELGFAGIERV VAVLREIAAV VPEGAAVTVD
AAELARTHPE AMVALRAEFA VMPGRFILRE
//
