ID A0A2K8ST34_9NOSO Unreviewed; 295 AA.
AC A0A2K8ST34;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=COO91_04606 {ECO:0000313|EMBL:AUB38634.1};
OS Nostoc flagelliforme CCNUN1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB38634.1, ECO:0000313|Proteomes:UP000232003};
RN [1] {ECO:0000313|EMBL:AUB38634.1, ECO:0000313|Proteomes:UP000232003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB38634.1,
RC ECO:0000313|Proteomes:UP000232003};
RA Shang J.;
RT "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT its photosynthetic adaptation to extreme terrestrial habitat.";
RL Submitted (NOV-2017) 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; CP024785; AUB38634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8ST34; -.
DR KEGG; nfl:COO91_04606; -.
DR Proteomes; UP000232003; 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 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:UP000232003}.
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 295 AA; 31569 MW; 8458037D5D596DE0 CRC64;
MNLSAWVQLA KIQAKQGRVA DRIPKLAKAN PDWFAAHICC KSGKTVSFGD TASFFPLMSV
IKTFSLLYLL EHFGAETVFG WVGVEPSDAP FNSLEQLIAD RGYPRNPMIN SGAITLADKL
TGKDASDRTL LFCQWLNQLA GCQLRLDEIM LASVRLTRST TNEAIANYLA KTSHLENPET
ALDTYEQICC ISGGVEDLAL LGKLLACENG CLSAQNRRIV NAVMSTCGLY EASAQFAVRV
GLPMKSGIGG GLVAIVPGEG AIACYSPTLD TVGNPVAGLA FVEALSQKLE LSIFG
//
