ID A0A1S1NCM0_9MYCO Unreviewed; 426 AA.
AC A0A1S1NCM0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:PQM47564.1};
GN ORFNames=BKN37_15390 {ECO:0000313|EMBL:OHV03073.1}, C1Y40_02233
GN {ECO:0000313|EMBL:PQM47564.1};
OS Mycobacterium talmoniae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1858794 {ECO:0000313|EMBL:OHV03073.1, ECO:0000313|Proteomes:UP000179734};
RN [1] {ECO:0000313|EMBL:OHV03073.1, ECO:0000313|Proteomes:UP000179734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MO-5499 {ECO:0000313|EMBL:OHV03073.1}, and NE-TNMC-100812
RC {ECO:0000313|Proteomes:UP000179734};
RA Greninger A.L., Elliott B., Vasireddy S., Vasireddy R.;
RT "Genome sequence of Mycobacterium talmonii.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PQM47564.1, ECO:0000313|Proteomes:UP000238296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2683 {ECO:0000313|EMBL:PQM47564.1,
RC ECO:0000313|Proteomes:UP000238296};
RX PubMed=28809146; DOI=10.1099/ijsem.0.001998;
RA Davidson R.M., DeGroote M.A., Marola J.L., Buss S., Jones V., McNeil M.R.,
RA Freifeld A.G., Elaine Epperson L., Hasan N.A., Jackson M., Iwen P.C.,
RA Salfinger M., Strong M.;
RT "Mycobacterium talmoniae sp. nov., a slowly growing mycobacterium isolated
RT from human respiratory samples.";
RL Int. J. Syst. Evol. Microbiol. 67:2640-2645(2017).
RN [3] {ECO:0000313|EMBL:PQM47564.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2683 {ECO:0000313|EMBL:PQM47564.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:OHV03073.1}.
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DR EMBL; MLQM01000082; OHV03073.1; -; Genomic_DNA.
DR EMBL; PPEA01000318; PQM47564.1; -; Genomic_DNA.
DR RefSeq; WP_071027347.1; NZ_MLQM01000082.1.
DR AlphaFoldDB; A0A1S1NCM0; -.
DR Proteomes; UP000179734; Unassembled WGS sequence.
DR Proteomes; UP000238296; 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 Gene3D; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
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.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 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:UP000179734}.
FT DOMAIN 315..397
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
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 158
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 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 426 AA; 44668 MW; 216E162A4176883B CRC64;
MADLVQSYLD RIVAEHAATA EGALADYIPE LAGVDPRGFG LSLSSGDGYV YETGDADIEF
TIQSVSKPFT YALALDQIGE AAVDARIGVE PSGEAFNEIS VDDVTKVPKN PMINAGAIAA
VSLIPGASPD ARFALIRDFY SACAGRQLPL DEAVYRSEKA TGSRNRAIAY MLDSFDVLDG
DPDEILDVYY RQCSLRVTST DLARMGATLA RAGVNPFTGR RVTNAAVVRR TLSVMLTCGM
YDAAGDWVSA VGMPAKSGVG GGIVAVLPGQ LGIGVYSPLL DAKGNSVRGV AVCRSLSAQL
GLHFLSVPLQ ARSTLRASYD VRDGVRVYEI HGDLLFAGAE QVLRMARQQS GEFSAAILDV
SRVDDINGAA RTMLAGLGAM LQAAGKRGFL VDPDGAVVSP GSPAQAVTFT TVDDAVAAAE
AWLFGR
//
