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Database: UniProt/TrEMBL
Entry: A0A0B6FWL5_YERFR
LinkDB: A0A0B6FWL5_YERFR
Original site: A0A0B6FWL5_YERFR 
ID   A0A0B6FWL5_YERFR        Unreviewed;       314 AA.
AC   A0A0B6FWL5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
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:AJI88872.1};
GN   ORFNames=AW19_2694 {ECO:0000313|EMBL:AJI88872.1};
OS   Yersinia frederiksenii Y225.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=1454377 {ECO:0000313|EMBL:AJI88872.1, ECO:0000313|Proteomes:UP000031898};
RN   [1] {ECO:0000313|EMBL:AJI88872.1, ECO:0000313|Proteomes:UP000031898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y225 {ECO:0000313|EMBL:AJI88872.1};
RX   PubMed=25931590;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G.,
RA   Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Coyne S.R.,
RA   Gibbons H.S., Lo C.C., Munk A.C., Rosenzweig C.N., Koroleva G.I.,
RA   Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT   "Thirty-Two Complete Genome Assemblies of Nine Yersinia Species,
RT   Including Y. pestis, Y. pseudotuberculosis, and Y. enterocolitica.";
RL   Genome Announc. 3:0-0(2015).
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; CP009364; AJI88872.1; -; Genomic_DNA.
DR   RefSeq; WP_038638896.1; NZ_CP009364.1.
DR   EnsemblBacteria; AJI88872; AJI88872; AW19_2694.
DR   KEGG; yfr:AW19_2694; -.
DR   KO; K01425; -.
DR   Proteomes; UP000031898; 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:UP000031898};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313,
KW   ECO:0000256|SAAS:SAAS00041473, ECO:0000313|EMBL:AJI88872.1}.
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   314 AA;  33059 MW;  7CA13D5C328F8B3E CRC64;
     MTINLARLNQ VINDVHSQYS MLAGGENASY IPYLASVPSQ LAGLAIVTVG GDIISQGDAD
     FRFALESISK VCSLALALED IGPQAVQDKI GADPTGLPFN SVIALELHNG KPLSPLVNAG
     AMSTVSAIKA SSREERWARI LDIQQQLAGA PIALSDEVNH SEQTTNFHNR AIAWLLYSAQ
     AMYCDPMEAC DVYTRQCSTL FSTIELATMG ATFAAGGRNP VTQKQVLTAS NMPYILAEMT
     MEGMYGSSGD WAYTVGLPGK SGVGGGILAV VPGVMGIAAF SPPLDPVGNS VRGQKMVASV
     AQQLGYNLYK GPLL
//
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