(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NYL4_YERPA

ID   A0A0E1NYL4_YERPA        Unreviewed;       308 AA.
AC   A0A0E1NYL4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 25.
DE   RecName: Full=Glutaminase {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00358860};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00313, ECO:0000256|SAAS:SAAS00358860};
GN   Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN   OrderedLocusNames=YPA_0315 {ECO:0000313|EMBL:ABG12283.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12283.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12283.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12283.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00313,
CC         ECO:0000256|SAAS:SAAS01120526};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00313,
CC       ECO:0000256|SAAS:SAAS01149771}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00313, ECO:0000256|SAAS:SAAS00551679}.
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DR   EMBL; CP000308; ABG12283.1; -; Genomic_DNA.
DR   RefSeq; WP_002209989.1; NZ_CP009906.1.
DR   SMR; A0A0E1NYL4; -.
DR   EnsemblBacteria; ABG12283; ABG12283; YPA_0315.
DR   EnsemblBacteria; AJJ81357; AJJ81357; CH58_3162.
DR   KEGG; ypa:YPA_0315; -.
DR   PATRIC; fig|360102.15.peg.3318; -.
DR   KO; K01425; -.
DR   OMA; TCGFYDE; -.
DR   Proteomes; UP000001971; 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;
DR   PRODOM; A0A0E1NYL4.
DR   SWISS-2DPAGE; A0A0E1NYL4.
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00313,
KW   ECO:0000256|SAAS:SAAS00436360, ECO:0000313|EMBL:ABG12283.1}.
FT   BINDING      66     66       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     117    117       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     161    161       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     168    168       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     192    192       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     244    244       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00313}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00313}.
SQ   SEQUENCE   308 AA;  33700 MW;  D80AD7C77F23FEC3 CRC64;
     MVTTLDNALL NDILQQVRPL IGQGKVADYI PALAEVPANK LGIAVCTLDG QIFQAGDADE
     RFSIQSISKV LSLTLALSRY SEQDIWQRVG KEPSGQPFNS LVQLELEKGK PRNPFINLGA
     LVVCDMLQSR LSAPKQRLLE VVRQLVKDDS ISYDPRVARS EFEHSDRNAA IAYLMKSFGN
     FDNDVLTVLQ TYFHYCAMRM SCVELARCFV YLANQGRSIS GSESLITPMQ ARQINALMIT
     SGMYDGAGEF AFRVGMPGKS GVGGGIIAIV PDEFCIAVWS PELDHAGNSL AGTAALERLA
     QQMGRSIF
//

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