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Database: UniProt/TrEMBL
Entry: A0A0U4IS22_SERFO
LinkDB: A0A0U4IS22_SERFO
Original site: A0A0U4IS22_SERFO 
ID   A0A0U4IS22_SERFO        Unreviewed;       312 AA.
AC   A0A0U4IS22;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-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=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN   ORFNames=AV650_23305 {ECO:0000313|EMBL:ALX96278.1};
OS   Serratia fonticola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:ALX96278.1, ECO:0000313|Proteomes:UP000061771};
RN   [1] {ECO:0000313|EMBL:ALX96278.1, ECO:0000313|Proteomes:UP000061771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS2 {ECO:0000313|EMBL:ALX96278.1,
RC   ECO:0000313|Proteomes:UP000061771};
RA   Shin J.-H., Jung B.K., Hong S.-J., Park G.-S.;
RT   "Complete genome sequence of Serratia fonticola GS2.";
RL   Submitted (JAN-2016) 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; CP013913; ALX96278.1; -; Genomic_DNA.
DR   RefSeq; WP_059201509.1; NZ_CP013913.1.
DR   EnsemblBacteria; ALX96278; ALX96278; AV650_23305.
DR   GeneID; 32348318; -.
DR   KEGG; sfg:AV650_23305; -.
DR   KO; K01425; -.
DR   Proteomes; UP000061771; 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:UP000061771};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313,
KW   ECO:0000256|SAAS:SAAS00041473}.
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   312 AA;  33100 MW;  027F178DC734208B CRC64;
     MTIDLQRLQQ VASNAYAQYS TLSGGENASY IPFLASVPSH LAALAIVTVD GDIISQGDAE
     FRFALESISK VCSLALALED VGPQDVQDKI GADPTGLPFN SVIALELHKG KPLSPLVNAG
     AMSTVSLVKA SDRENRWLRI LDMQQQLAGA QIALSDEVND SEQSTNFHNR AIAWLLYSAD
     AMYCDPMEAC DVYTRQCSTL LNTIELATMG ATIAAGGINP VSKKRVLTES NTPFILAEMT
     MEGMYGSSGD WAYTVGLPGK SGVGGGILTV VPGVMGIAAF SPPLDPVGNS VRGQKMVAAV
     AQQMGYNLYR SR
//
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