ID A0A2A4G0M5_9SPHN Unreviewed; 318 AA.
AC A0A2A4G0M5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=COO09_04350 {ECO:0000313|EMBL:PCE43541.1};
OS Rhizorhabdus dicambivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=1850238 {ECO:0000313|EMBL:PCE43541.1, ECO:0000313|Proteomes:UP000218934};
RN [1] {ECO:0000313|EMBL:PCE43541.1, ECO:0000313|Proteomes:UP000218934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ndbn-20m {ECO:0000313|EMBL:PCE43541.1,
RC ECO:0000313|Proteomes:UP000218934};
RA Na L.;
RT "The Catabolism of 3,6-Dichlorosalicylic acid is Initiated by the
RT Cytochrome P450 Monooxygenase DsmABC in Rhizorhabdus dicambivorans
RT Ndbn-20.";
RL Submitted (SEP-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: 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:PCE43541.1}.
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DR EMBL; NWUF01000003; PCE43541.1; -; Genomic_DNA.
DR RefSeq; WP_066960166.1; NZ_NWUF01000003.1.
DR AlphaFoldDB; A0A2A4G0M5; -.
DR KEGG; rdi:CMV14_02030; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000218934; 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:UP000218934}.
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 119
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 318 AA; 33919 MW; 9CA3F2A7B3C1F334 CRC64;
MPVTAAPDLQ AIIDRIAEEM AGQADRGKVA DYIPGLARVD PKHFGISIAT HDGKMYSAGD
AAMPFSIQSV SKVFALTIAL GKVGDSLWQR VGREPSGNAF NSIVQLEAEH GIPRNPFINA
GAIVVADVIL AGHQPKEAIG EILRFVRQIA GDDGIMIDDE VAKGEAETGF RNAALANYMR
SFGNIHHPVE QVLGVYFHQC ALTMTCEQLA RAGRYLMLEG QHPDTGFNVI SPMRARRINA
LMMLCGHYDG SGEFAFRVGI PGKSGVGGGI MLIVPGIASI AVWSPGLNDR GNSTLGSLAL
ERLAVATGWS VFNQREPG
//
