ID A0A067Z6A6_GLUOY Unreviewed; 318 AA.
AC A0A067Z6A6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ECO:0000313|EMBL:AHK72048.1};
GN ORFNames=GLS_c21770 {ECO:0000313|EMBL:AHK72048.1};
OS Gluconobacter oxydans DSM 3504.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1288313 {ECO:0000313|EMBL:AHK72048.1, ECO:0000313|Proteomes:UP000031656};
RN [1] {ECO:0000313|EMBL:AHK72048.1, ECO:0000313|Proteomes:UP000031656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3504 {ECO:0000313|EMBL:AHK72048.1};
RX PubMed=25267158; DOI=10.1007/s00253-014-6069-9;
RA Kostner D., Luchterhand B., Junker A., Volland S., Daniel R., Buchs J.,
RA Liebl W., Ehrenreich A.;
RT "The consequence of an additional NADH dehydrogenase paralog on the growth
RT of Gluconobacter oxydans DSM3504.";
RL Appl. Microbiol. Biotechnol. 99:375-386(2015).
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}.
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DR EMBL; CP004373; AHK72048.1; -; Genomic_DNA.
DR RefSeq; WP_011253579.1; NZ_CP004373.1.
DR AlphaFoldDB; A0A067Z6A6; -.
DR SMR; A0A067Z6A6; -.
DR GeneID; 56906403; -.
DR KEGG; goy:GLS_c21770; -.
DR HOGENOM; CLU_027932_1_1_5; -.
DR Proteomes; UP000031656; 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}.
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 318 AA; 34315 MW; 11F5C022D148E793 CRC64;
MSTVASIIVS IAEEMRTASE RGTVANYIPP LARVDLNRFG MAVVGMDGET HTVGDAEVPF
SVQSVSKVFS LSMALNAMGD ELWGRVRQEP SGSAFNSIVQ LENEHGIPRN PFINAGAIVI
ADILVSRYGR ENAQTRLLEF LRPLVSDPSS IDIDTDVARQ ERETGFRNMA LANYMRTFGN
IRNVVEDTLD FYFHQCALTM SCHQLAQVGT CLMTGGRNPL TGERIMSERN AQTILALMMM
CGHYDGSGAF AIRVGLPGKS GVGGGILAIA PGVASIAVWS PGLNAQGNSL LGTRALERLV
QHTGWSVFRA NPWVANPT
//
