GLSA_OCEIH
ID GLSA_OCEIH Reviewed; 331 AA.
AC Q8CV87;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=OB0870;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12826.1; -; Genomic_DNA.
DR RefSeq; WP_011065276.1; NC_004193.1.
DR AlphaFoldDB; Q8CV87; -.
DR SMR; Q8CV87; -.
DR STRING; 221109.22776551; -.
DR EnsemblBacteria; BAC12826; BAC12826; BAC12826.
DR KEGG; oih:OB0870; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_9; -.
DR OMA; RNPMINS; -.
DR OrthoDB; 1288854at2; -.
DR PhylomeDB; Q8CV87; -.
DR Proteomes; UP000000822; 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..331
FT /note="Glutaminase"
FT /id="PRO_0000110614"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 331 AA; 36507 MW; BE3AF061D2DC229F CRC64;
MVQGSVNLNT ERGKEWLQDY VDNWVNFYQK QTDEGKVASY IPRLEHADPN ALGISIIGKN
GTVIRSGDTD LEFSIQSISK VLSFIVACME RGLSYVLQRV DVEPTGESFN SIMHLEINQP
KKPFNPLVNS GAITVSSLLN GRTSDQKLEP LYQLLEKILG HRPEIDVEVY VSERDTSMRN
RAIGYYLLEE GYLESDLSIT LETYFKHCSL NVTVDDLAMI GLVLSNDGVH PNTDEPLIPK
QIARVAKSLM LTCGMYDASG KFASYVGIPA KSGVSGGILA VVPPRVRDQN LPFLEGCGIG
VFGPALDKQG NSIAGIKLLR HIANQWDLSL F