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Database: UniProt
Entry: J9S649_9ACTN
LinkDB: J9S649_9ACTN
Original site: J9S649_9ACTN 
ID   J9S649_9ACTN            Unreviewed;       477 AA.
AC   J9S649;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=KTR9_1881 {ECO:0000313|EMBL:AFR48520.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48520.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR48520.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR48520.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(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; CP002907; AFR48520.1; -; Genomic_DNA.
DR   RefSeq; WP_014926358.1; NC_018581.1.
DR   AlphaFoldDB; J9S649; -.
DR   STRING; 337191.KTR9_1881; -.
DR   KEGG; gor:KTR9_1881; -.
DR   PATRIC; fig|337191.3.peg.2158; -.
DR   eggNOG; COG0659; Bacteria.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_0_0_11; -.
DR   Proteomes; UP000003281; 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   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}.
FT   DOMAIN          351..466
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         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   477 AA;  51665 MW;  7533A55C9EFCCC69 CRC64;
     MRSLVDGYLS HIMDECHSDR SGHVADYIPE LAAVDPEGYG LSLCVHDGHT YSQGDSATSF
     TIQSVSKPLT YAMILKKHGT AAVDAKIGVE PSGEAFNEIS VDDRRRPKNP MINAGAIFAA
     SMLLPPTRDV DDAAVDAAFR EVLEFYSGCA GRHLVMDEEV YASEAATGSR NRAIAYMLDS
     FGALETSPDA ALDLYYRQCS IRVTTDDLAG IGATIGNGGM NPRTGRTVFS NETAQRLLSV
     MTTCGMYDGA GDWVTSVGLP AKSGVGGGIL AVLPGQLGIG VYSPRLDAHG NSVRGVDVCR
     HLSTDLGLHM FNVTRESRVT IRSVYDLADT PVSAEWGEQE RSYLRTCRDR IRVYELQGDL
     TFAGAESVQR RLEADLDDYT VVIVEISRIG VIDAVARTMV LSIKRLLDDS GRRAALVDPD
     GVVRSSVDRH RNDAAVPDLD APPELQGFDP ALPHVHSTMD DAVIDAETFL LKHYYDQ
//
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