ID F7RZR6_9GAMM Unreviewed; 313 AA.
AC F7RZR6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=A28LD_1938 {ECO:0000313|EMBL:EGN74921.1};
OS Idiomarina sp. A28L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN74921.1, ECO:0000313|Proteomes:UP000053031};
RN [1] {ECO:0000313|EMBL:EGN74921.1, ECO:0000313|Proteomes:UP000053031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A28L {ECO:0000313|EMBL:EGN74921.1,
RC ECO:0000313|Proteomes:UP000053031};
RX PubMed=21742887; DOI=10.1128/JB.05648-11;
RA Gupta H.K., Singh A., Sharma R.;
RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT India.";
RL J. Bacteriol. 193:5875-5876(2011).
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:EGN74921.1}.
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DR EMBL; AFPO01000021; EGN74921.1; -; Genomic_DNA.
DR RefSeq; WP_007420903.1; NZ_AFPO01000021.1.
DR AlphaFoldDB; F7RZR6; -.
DR STRING; 1036674.A28LD_1938; -.
DR PATRIC; fig|1036674.4.peg.1936; -.
DR eggNOG; COG2066; Bacteria.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000053031; 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:UP000053031}.
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 313 AA; 33857 MW; 0685307816B7D28D CRC64;
MEGTPQQPKN CASLLEQLVA EARKASPGGQ VADYIPALAQ VDAEHVGIAV VELDGTVHTA
GDANMPFSIQ SISKIFGLAL AMDRMDDTLW ERVRMEPSGQ AFNSIVQLEW EHGIPRNPFI
NAGAIVVADV LTSRYSSSKT AFVQYVRQLC GNETIHADHD VWNSEKEHGN RNAALAYLMK
SFGNIDSSVP EVLDHYFFQC SIAMSCVDLA RSLGFLANKG IQPGTEQRVC DARSAHRINA
LLSTSGMYDQ SGEFAFTVGL PAKSGVGGGI IAVVPDYGVI CAWSPPLNRF GNPARAVEMI
TQFALRLGLS VYH
//
