ID A0A2M9JU22_9ACTN Unreviewed; 600 AA.
AC A0A2M9JU22;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:PJN10363.1};
GN ORFNames=CG723_18505 {ECO:0000313|EMBL:PJN10363.1};
OS Streptomyces sp. CB01635.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN10363.1, ECO:0000313|Proteomes:UP000232157};
RN [1] {ECO:0000313|Proteomes:UP000232157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN10363.1}.
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DR EMBL; NNBL01000005; PJN10363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9JU22; -.
DR Proteomes; UP000232157; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
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 Pfam; PF01740; STAS; 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:UP000232157}.
FT DOMAIN 358..431
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 319..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 600 AA; 63615 MW; 0FC2AA95FEBF1A81 CRC64;
MVFDCGVRHN KPLDDPLAAL LDRVRIRLRD LTDGEPASYI PELSRADPDL FGLSLCALDG
QVYSCGDSEV PFTVQSVSKP FVFALALADQ GLEDVLARVG AEPSGEGFSS IRLEPGTGRP
PNPMVNAGAI VTSSLVAGAN PDERIGRILA GLGAFAGRDL TVDEAVFASE RSTGDRNRAL
AYLMHNAGSL TGDVEEQLAV YFRQCSVLVT CDDLAVMHAT LAGGGTNPLT GERVVASRHA
QHVLAVMATC GMYDASGQWM LRVGLPAKSG VSGGIGVALP GQFGIGVFSP PLDEKGNSVR
AIAACHLLSE QFGLHLMRAT GSSGRPLPPR SLDPGPLRSL RHRPRDQRAA LDERPDRIRV
HVLQGDLDFA TAEQTLRAAR DLPKAARWFV LDLARVGRIE PVAADLLRAL GHDLRERGIR
MVIADPSARP VTHTKDEFAD LGRAIESCED ELLTGLGLDP SVPVPLTDSD LFGRAGEQAA
QAVFDCFGTM SLSAGQAVEP PRAEPVVLWY VESGRLAVCA HSSRPTPAGR TWSAGPGAAL
TPADFHARLG ERVMAEEDSV CRTLTAAGLL RLRTAVPAAA AFLERSPLDG AETVDRPEGA
//
