ID A0A1Y2MK54_PSEAH Unreviewed; 413 AA.
AC A0A1Y2MK54;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:OSY35610.1};
GN ORFNames=BG845_05945 {ECO:0000313|EMBL:OSY35610.1};
OS Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS autotrophica).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY35610.1, ECO:0000313|Proteomes:UP000194360};
RN [1] {ECO:0000313|EMBL:OSY35610.1, ECO:0000313|Proteomes:UP000194360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 535 {ECO:0000313|EMBL:OSY35610.1,
RC ECO:0000313|Proteomes:UP000194360};
RA Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT potential of specific P450 cytochromes.";
RL Submitted (SEP-2016) 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:OSY35610.1}.
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DR EMBL; MIGB01000049; OSY35610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2MK54; -.
DR STRING; 2074.BG845_05945; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000194360; 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; 2.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
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.
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:UP000194360}.
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 413 AA; 43445 MW; 21D87B60DC9660AE CRC64;
MRTPVPDYLA EVLDGVVADR SGRVADYIPD LADADPEVLG VAVTTVAGRT YAAGDADVEF
SIQSISKPFA YAAALTDRGT EVVDATVGVE PSGEAFDELS LEGGTHRPKN PMINAGAIAV
HHLLVGPDAT GAARVERVVD FFSELAGRRL TVDESVYRSE LDTADRNLAI AHMLRNYRVL
SEPAAEVVDG YTRQCAVNVT VRDLAMMGAT LANAGVHPVT GRRVLPAAVA RRTMSVMAGS
GMYDGAGDWL VRVGIPAKSG VAGGMLGALP GQLGLATVSP RLDAHGNSVR GVAICERLSR
DMGMHLMEAE PYGSTVLRGT RVDGDATVVA LQGAVQFSGA EAVLDRLATE PISTPEVVLD
LSRVDRFSDV GRRMTLEGLR RLTLDGHTVA VIDPDGVLPD PDLGDGTRAQ LRT
//
