ID E6JD42_9ACTN Unreviewed; 418 AA.
AC E6JD42;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=ES5_15816 {ECO:0000313|EMBL:EFV90484.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV90484.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV90484.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV90484.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(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}.
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:EFV90484.1}.
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DR EMBL; AEKG01000376; EFV90484.1; -; Genomic_DNA.
DR RefSeq; WP_007633131.1; NZ_AEKG01000376.1.
DR AlphaFoldDB; E6JD42; -.
DR Proteomes; UP000004165; 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; PF13466; STAS_2; 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 318..394
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 389..418
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 418 AA; 44838 MW; 0563F7096084908C CRC64;
MKTPVPDYLL EIRDACSDGG EGRLADYIPE LAAVDPDRFA VAACTMDGVV YTAGDADAEF
TIQSMSKPFV YALALRDRGI EAVLEKVEVE PSGDAFNQIS LNRDTGRPRN PMINIGAITT
HTLVGSPGAS EDERSEVIAD GLSAFAGRRL EVDGAVCESE LRTAFRNRAM ANLVRAGGII
EDDPDEAVRG YTRQCAYQVT VRDLAVMAVT LATGGVNPVT RERVVSAPVA RQVLAVMATC
GMYDAAGDWM STVGIPAKSG VSGGILGALP GQVGLGVFSP RLDEHGHSVE GVRTFERLSQ
DLELHLMNTT VTEVEAVRSV RFDEISGRRT FRLQGPMTFA SAEQVLRRLA EIPEGPGEVT
LDLSRVSSVN TSARRMLLEA MRRLSAEGHT VGLADPGRRL PEPDLGDGTR PVTRRAAR
//
