GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0H3DW01_EDWTF
LinkDB: A0A0H3DW01_EDWTF
Original site: A0A0H3DW01_EDWTF 
ID   A0A0H3DW01_EDWTF        Unreviewed;       311 AA.
AC   A0A0H3DW01;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-SEP-2017, entry version 13.
DE   RecName: Full=Glutaminase {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00041476};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00041476};
GN   Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN   OrderedLocusNames=ETAF_2602 {ECO:0000313|EMBL:ADM42704.1};
OS   Edwardsiella tarda (strain FL6-60).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=718251 {ECO:0000313|EMBL:ADM42704.1, ECO:0000313|Proteomes:UP000002230};
RN   [1] {ECO:0000313|Proteomes:UP000002230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FL6-60 {ECO:0000313|Proteomes:UP000002230};
RA   van Soest J.J., Henkel C.V., Jansen H.J., van den Hondel C.A.M.J.J.,
RA   Bloemberg G.V., Meijer A.H., Spaink H.P.;
RT   "Genome comparisons of Edwardsiella bacteria analysed using deep
RT   sequencing technology.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC       {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00062832}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00313,
CC       ECO:0000256|SAAS:SAAS00551681}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00313, ECO:0000256|SAAS:SAAS00551679}.
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DR   EMBL; CP002154; ADM42704.1; -; Genomic_DNA.
DR   RefSeq; WP_012849689.1; NC_017309.1.
DR   ProteinModelPortal; A0A0H3DW01; -.
DR   EnsemblBacteria; ADM42704; ADM42704; ETAF_2602.
DR   KEGG; etd:ETAF_2602; -.
DR   PATRIC; fig|718251.5.peg.2703; -.
DR   KO; K01425; -.
DR   OMA; MYTCGMY; -.
DR   Proteomes; UP000002230; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   PANTHER; PTHR12544; PTHR12544; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002230};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313,
KW   ECO:0000256|SAAS:SAAS00041473, ECO:0000313|EMBL:ADM42704.1}.
FT   BINDING      67     67       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     118    118       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     169    169       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     193    193       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     263    263       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00313}.
SQ   SEQUENCE   311 AA;  32799 MW;  CDAC5FCCB34A9F17 CRC64;
     MTLDAQRLQQ AVDAAHAQYA TLAGGKNADY IPYLASVPSQ LAAVAVVTRD GAVYCAGDSD
     YRFALESISK VCTLALALED VGPEAVQEKI GADPTGLPFN SVMALELHGG KPLSPLVNAG
     AMASASLIKA DNREQRWQRI LAIQQQLAGE TVALSDEVNQ SEQTTNFHNR AIAWLLYSAG
     TMYCDPMEAC DVYTRQCSTL IDTVELATLG ATLAAGGVNP RSGRRVLQAD NVPYILAEMT
     MEGLYGRSGD WAYRVGLPGK SGVGGGILAV VPGVMGIAAF SPPLDEAGNS VRGRKMVADV
     AARLGYNLYK A
//
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