GenomeNet

Database: UniProt/SWISS-PROT
Entry: GLSA_MYCUA
LinkDB: GLSA_MYCUA
Original site: GLSA_MYCUA 
ID   GLSA_MYCUA              Reviewed;         320 AA.
AC   A0PTH3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313};
DE            EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN   Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313};
GN   OrderedLocusNames=MUL_3484;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L.,
RA   Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C.,
RA   Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
CC       {ECO:0000255|HAMAP-Rule:MF_00313}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313}.
CC   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00313}.
DR   EMBL; CP000325; ABL05642.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0PTH3; -.
DR   SMR; A0PTH3; -.
DR   EnsemblBacteria; ABL05642; ABL05642; MUL_3484.
DR   KEGG; mul:MUL_3484; -.
DR   HOGENOM; HOG000216890; -.
DR   KO; K01425; -.
DR   OMA; MYTCGMY; -.
DR   OrthoDB; POG091H02PU; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
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   Complete proteome; Hydrolase.
FT   CHAIN         1    320       Glutaminase.
FT                                /FTId=PRO_0000336032.
FT   BINDING      70     70       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     121    121       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     165    165       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     172    172       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     196    196       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     248    248       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     266    266       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00313}.
SQ   SEQUENCE   320 AA;  33748 MW;  538A7317BF2254ED CRC64;
     MAPTSVSNAR IEKAVLDAHE KQKNKHGGKN ADYIPILAQV PSTLFGVSVA TVDGQVFTAG
     DAGYEFALES ISKIFTLALV IEQRGPRELR LKVGADPTGE AFNSVLALEL HNDKPMSPLV
     NAGAISTTSL VDAVGPEDRW RQIVGAQSDF AGRQISISEE INASEQATNF HNRAIAWLLR
     GSGYIYCDPM EACDIYTRQC STLVTTADLA VMGATLANGG TNPITGKRVI ARKNVPHVLA
     EMTMEGVYTR SGDWAYTVGL PAKSGVGGGL VAVAPGQLAI AAFSPPLDKV GNSVRAQAAV
     AQIADTLQLG LFNVPGEEDE
//
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