GLSA2_ALKHC
ID GLSA2_ALKHC Reviewed; 324 AA.
AC Q9K9D1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Glutaminase 2 {ECO:0000255|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN Name=glsA2 {ECO:0000255|HAMAP-Rule:MF_00313}; OrderedLocusNames=BH2717;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06436.1; -; Genomic_DNA.
DR PIR; E83989; E83989.
DR RefSeq; WP_010898865.1; NC_002570.2.
DR AlphaFoldDB; Q9K9D1; -.
DR SMR; Q9K9D1; -.
DR STRING; 272558.10175338; -.
DR PRIDE; Q9K9D1; -.
DR EnsemblBacteria; BAB06436; BAB06436; BAB06436.
DR KEGG; bha:BH2717; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_9; -.
DR OMA; RNPMINS; -.
DR OrthoDB; 1288854at2; -.
DR Proteomes; UP000001258; 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..324
FT /note="Glutaminase 2"
FT /id="PRO_0000110593"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 324 AA; 35506 MW; 03B9D3F716B01474 CRC64;
MLQQKQSLLE HKPVLSKELE KLVNHYRTLS LNGQCAQYIP ALREANQTYL GLYVVHSNGI
EIKSGDWQVP FTLQSISKII NFIAACLDRG ITYVLDRVDV EPTGDPFNSM VRLEMRKTGK
PFNPMINAGA ITVASLLSGK SPTEKLESVY SLVEKMLGRR ASANEAVFHS EWQTAHRNRS
LAYYLKDTGY LESEVDDALH VYFTLCAIEV ATKDIAKIGL ILANNGYDPL SHQQIFPKEV
AKLTKALMLT CGMYNASGTF AAHIGIPAKS GVSGGIMAAV PARGRSDEAM GIGIYGPAID
DFGNSVAGVA LLKHLSHMWD LSIF
