ID A0A0U3MCD2_STRGL Unreviewed; 447 AA.
AC A0A0U3MCD2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=WQO_33510 {ECO:0000313|EMBL:ALU97834.1};
OS Streptomyces globisporus C-1027.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172567 {ECO:0000313|EMBL:ALU97834.1, ECO:0000313|Proteomes:UP000064183};
RN [1] {ECO:0000313|EMBL:ALU97834.1, ECO:0000313|Proteomes:UP000064183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-1027 {ECO:0000313|EMBL:ALU97834.1,
RC ECO:0000313|Proteomes:UP000064183};
RX PubMed=22815456; DOI=10.1128/JB.00797-12;
RA Wang L., Wang S., He Q., Yu T., Li Q., Hong B.;
RT "Draft genome sequence of Streptomyces globisporus C-1027, which produces
RT an antitumor antibiotic consisting of a nine-membered enediyne with a
RT chromoprotein.";
RL J. Bacteriol. 194:4144-4144(2012).
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}.
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DR EMBL; CP013738; ALU97834.1; -; Genomic_DNA.
DR RefSeq; WP_010062548.1; NZ_CP013738.1.
DR AlphaFoldDB; A0A0U3MCD2; -.
DR STRING; 1172567.WQO_33510; -.
DR KEGG; sgb:WQO_33510; -.
DR Proteomes; UP000064183; Chromosome.
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}.
FT DOMAIN 332..396
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 400..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 447 AA; 47350 MW; CD58F34F73F4A1C1 CRC64;
MRSIIPDYLT EVLAGVQPEA SGEPAGYIPE LAAADPERLS AAFAMIDGEV YGAGDIDTEF
TIQSISKPFA YALALADRGF APVLAKVGVE PSGEAFNEIS LESDTGRPRN PMINAGAITV
HSLVGPEGLN ATERVERVVD GLSAFAGRRL RTDDAVHASE MKHAHRNLAI AHMLRSHDIL
VGDARAVVDG YTRQCSVLVS TRDLAMMAAT LANRGMNPLS GEQVVPEPVV RQVLSVMFGC
GMYDAAGDWG TQVGIPAKSG VAGGLIGALP GQVGIATFSP RLDNHGNSVR GVKLFERFSS
DMGLHVMEVP ATARAALRTN HVAGSGPDAF RVLQLQDGIG FAGAERVIRE TVNTSYPETS
IALDLTRVHS IDDVARRMLL EIMRRLTLDG HEVYLVDPES IMPDPDPGDG GRVTVVDSLD
EASGSKTPPT PAARRRISGS AGTARRT
//
