ID A0A081FZJ0_9GAMM Unreviewed; 333 AA.
AC A0A081FZJ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ADIMK_1916 {ECO:0000313|EMBL:KEA63945.1};
OS Marinobacterium lacunae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA63945.1, ECO:0000313|Proteomes:UP000028252};
RN [1] {ECO:0000313|EMBL:KEA63945.1, ECO:0000313|Proteomes:UP000028252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK27 {ECO:0000313|EMBL:KEA63945.1,
RC ECO:0000313|Proteomes:UP000028252};
RA Singh A., Pinnaka A.K.;
RT "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT collected from Kochi backwaters in Kerala, India.";
RL Submitted (APR-2014) 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: 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:KEA63945.1}.
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DR EMBL; JMQN01000023; KEA63945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081FZJ0; -.
DR STRING; 1232683.ADIMK_1916; -.
DR PATRIC; fig|1232683.4.peg.1885; -.
DR eggNOG; COG2066; Bacteria.
DR Proteomes; UP000028252; 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:UP000028252}.
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 333 AA; 36262 MW; 906DFFAC780AC367 CRC64;
MPFMMYENLS GAQRVAARPI ADARALQDWV ESIDTRARER LGQGRVADYI PALAEQDPSR
FGIAICTTDG EVYAAGDAQD SFSIQSISKV FLLTLSLRIF GNDLWERVGL NPSGMPFNSL
SQLEVERGKP RNPFINAGAI VVTDHLVSAY AAPSQYLQDV VRRLSGNNSV LIDRRVLDSE
WQHRSRNAAM AYLMKSFGNI GNEVDDVLYA YFACCALGMS CVDLAVAFNY LAASGYSRMA
DERIIEPELS RKINSIMFTS GMYDAAGEFA YRVGLPAKSG VGGGILAVVP GRLSVCVWSP
ALDGNGNSVA GQYALELLSD ELDRMLPARV STD
//
