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Database: UniProt/TrEMBL
Entry: A0A076LLE6_9GAMM
LinkDB: A0A076LLE6_9GAMM
Original site: A0A076LLE6_9GAMM 
ID   A0A076LLE6_9GAMM        Unreviewed;       311 AA.
AC   A0A076LLE6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 18.
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   ECO:0000313|EMBL:AIJ07552.1};
GN   ORFNames=ETEE_1089 {ECO:0000313|EMBL:AIJ07552.1};
OS   Edwardsiella anguillarum ET080813.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=667120 {ECO:0000313|EMBL:AIJ07552.1, ECO:0000313|Proteomes:UP000028681};
RN   [1] {ECO:0000313|EMBL:AIJ07552.1, ECO:0000313|Proteomes:UP000028681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=080813 {ECO:0000313|Proteomes:UP000028681};
RX   PubMed=22590641; DOI=10.1371/journal.pone.0036987;
RA   Yang M., Lv Y., Xiao J., Wu H., Zheng H., Liu Q., Zhang Y., Wang Q.;
RT   "Edwardsiella comparative phylogenomics reveal the new intra/inter-
RT   species taxonomic relationships, virulence evolution and niche
RT   adaptation mechanisms.";
RL   PLoS ONE 7:e36987-E36987(2012).
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:SAAS00559507}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00313, ECO:0000256|SAAS:SAAS00551679}.
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DR   EMBL; CP006664; AIJ07552.1; -; Genomic_DNA.
DR   RefSeq; WP_034164627.1; NZ_CP006664.1.
DR   EnsemblBacteria; AIJ07552; AIJ07552; ETEE_1089.
DR   GeneID; 33938774; -.
DR   KEGG; ete:ETEE_1089; -.
DR   KO; K01425; -.
DR   Proteomes; UP000028681; 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:UP000028681};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313,
KW   ECO:0000256|SAAS:SAAS00041473, ECO:0000313|EMBL:AIJ07552.1}.
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;  32785 MW;  7474811EA0E96D4F CRC64;
     MTLDAQKLQQ AVDAAHAQYA TLVGGKNADY IPYLASVPSQ LAAVAVVTRD GAVYCAGDSG
     YRFALESISK VCTLALALED VGPEAVQDKI GADPTGLPFN SVMALELHGD KPLSPLVNAG
     AMASASLIKA DNREQRWQRI LAIQQQLAGE TVALSDEVNQ SEQTTNFHNR AIAWLLYSAG
     TMYCDPMEAC DVYTRQCSTL IDTVELATLG ATLAAGGVNP RSGRRVLQVD NVPYILAEMT
     MEGLYGRSGD WAYRVGLPGK SGVGGGILAV VPGVMGIAAF SPPLDEAGNS VRGQKMVADV
     AARLGYNLYK A
//
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