ID A0A0G1WA09_9BACT Unreviewed; 198 AA.
AC A0A0G1WA09;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=UY16_C0036G0005 {ECO:0000313|EMBL:KKU87163.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_47_9.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618445 {ECO:0000313|EMBL:KKU87163.1, ECO:0000313|Proteomes:UP000034739};
RN [1] {ECO:0000313|EMBL:KKU87163.1, ECO:0000313|Proteomes:UP000034739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000256|ARBA:ARBA00008345}.
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:KKU87163.1}.
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DR EMBL; LCOY01000036; KKU87163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1WA09; -.
DR PATRIC; fig|1618445.3.peg.939; -.
DR Proteomes; UP000034739; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002161; PdxT/SNO.
DR InterPro; IPR021196; PdxT/SNO_CS.
DR NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR Pfam; PF01174; SNO; 1.
DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS01236; PDXT_SNO_1; 1.
DR PROSITE; PS51130; PDXT_SNO_2; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW ECO:0000313|EMBL:KKU87163.1}; Transferase {ECO:0000313|EMBL:KKU87163.1}.
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT BINDING 57..59
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 114
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 140..141
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
SQ SEQUENCE 198 AA; 22106 MW; FF5B9BF95FA93D79 CRC64;
MRKKKIRIGI LAFQGGVAEH KEASLQALKN LKQDGEVVLI RSRKDIKNLD ALILPGGEST
VFYKLVLNAG IFQELKKIKN IFGTCAGAIF IAKNIKNKIK GQKSLEVMDM EVDRNAYGAQ
GESFEENIET KLGKINAVFI RAPKIKKVGK NVTILAGNKK NIIACEERGK GRNYLATCFH
PELSTTKFHE YFIKNLVL
//
