GenomeNet

Database: UniProt
Entry: N9PDX8_9GAMM
LinkDB: N9PDX8_9GAMM
Original site: N9PDX8_9GAMM 
ID   N9PDX8_9GAMM            Unreviewed;       425 AA.
AC   N9PDX8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=F895_02740 {ECO:0000313|EMBL:ENX13012.1};
OS   Acinetobacter sp. CIP 64.2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217694 {ECO:0000313|EMBL:ENX13012.1, ECO:0000313|Proteomes:UP000013107};
RN   [1] {ECO:0000313|EMBL:ENX13012.1, ECO:0000313|Proteomes:UP000013107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 64.2 {ECO:0000313|EMBL:ENX13012.1,
RC   ECO:0000313|Proteomes:UP000013107};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 64.2.";
RL   Submitted (FEB-2013) 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:ENX13012.1}.
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DR   EMBL; APRT01000018; ENX13012.1; -; Genomic_DNA.
DR   RefSeq; WP_005242810.1; NZ_KB850122.1.
DR   AlphaFoldDB; N9PDX8; -.
DR   STRING; 1217694.F895_02740; -.
DR   PATRIC; fig|1217694.3.peg.2659; -.
DR   HOGENOM; CLU_027932_0_0_6; -.
DR   Proteomes; UP000013107; 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}.
FT   DOMAIN          316..398
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         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   425 AA;  46795 MW;  C7DA9AECFF06757B CRC64;
     MKTPLPDYLA HVIDACDIDN SGHLADYIPE LANANPNRLA LALSTVDGEI YSVGDDEIEF
     TIQSMSKPFT YAYVLQQLGI DAVLEKVGVE PSGEAFNEIS LGKDRRPKNP MINSGAITTH
     SLIPAKEDVS GAEILRRFMS ELAGRELQFD DAVYESEVKT AYRNLSIGYM LRTVGILESD
     PEEIVNGYIR QCAILVTVKD LVRMGSVFAN GGVDPKTGKR LLNRAVVRQV LSVMMSCGMY
     DAAGDWLTTV GIPAKSGVAG GILGVLPGQV SIAAFSPRLD EHGNSIRGID ILERLSRDMG
     LHLMEGTPSA QTIVQSHYRT GKDASLSVYV LRGVLKFTEA EMLLRTLQCE PVDKSSIVID
     LTQISLIHEV GKRMFLEGID RLIDDGHSLL LVDPEQRLDH ARTHKDRVLH VYQNLEDLIE
     KHKEL
//
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