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Database: UniProt/TrEMBL
Entry: A0A0T9PMN2_YERKR
LinkDB: A0A0T9PMN2_YERKR
Original site: A0A0T9PMN2_YERKR 
ID   A0A0T9PMN2_YERKR        Unreviewed;       314 AA.
AC   A0A0T9PMN2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 11.
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=glsA1_2 {ECO:0000313|EMBL:CNH73027.1};
GN   Synonyms=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN   ORFNames=ERS008500_02997 {ECO:0000313|EMBL:CNH73027.1};
OS   Yersinia kristensenii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=28152 {ECO:0000313|EMBL:CNH73027.1, ECO:0000313|Proteomes:UP000044230};
RN   [1] {ECO:0000313|EMBL:CNH73027.1, ECO:0000313|Proteomes:UP000044230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FE80982 {ECO:0000313|EMBL:CNH73027.1,
RC   ECO:0000313|Proteomes:UP000044230};
RA   Murphy D.;
RL   Submitted (MAR-2015) 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: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; CQAQ01000007; CNH73027.1; -; Genomic_DNA.
DR   RefSeq; WP_038638896.1; NZ_CWJK01000008.1.
DR   EnsemblBacteria; CNH73027; CNH73027; ERS008500_02997.
DR   KEGG; ykr:CH54_3094; -.
DR   PATRIC; fig|28152.8.peg.3165; -.
DR   KO; K01425; -.
DR   Proteomes; UP000044230; Unassembled WGS sequence.
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:UP000044230};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313,
KW   ECO:0000256|SAAS:SAAS00041473, ECO:0000313|EMBL:CNH73027.1}.
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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