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Database: UniProt/TrEMBL
Entry: E8MGJ7_BIFL2
LinkDB: E8MGJ7_BIFL2
Original site: E8MGJ7_BIFL2 
ID   E8MGJ7_BIFL2            Unreviewed;       513 AA.
AC   E8MGJ7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   19-FEB-2014, entry version 22.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.-;
GN   Name=gatA; OrderedLocusNames=BLLJ_0230;
OS   Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 /
OS   JCM 1217 / NCTC 11818 / E194b).
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=565042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K.,
RA   Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K.,
RA   Kikuchi J., Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in
CC       organisms which lack glutaminyl-tRNA synthetase. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated gamma-phospho-Glu-tRNA(Gln) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
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DR   EMBL; AP010888; BAJ65900.1; -; Genomic_DNA.
DR   RefSeq; YP_004219992.1; NC_015067.1.
DR   ProteinModelPortal; E8MGJ7; -.
DR   EnsemblBacteria; BAJ65900; BAJ65900; BLLJ_0230.
DR   GeneID; 10208996; -.
DR   KEGG; blm:BLLJ_0230; -.
DR   PATRIC; 46888696; VBIBifLon48544_0237.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   OMA; FGYRCEN; -.
DR   BioCyc; BLON565042:GIWN-238-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   TIGRFAMs; TIGR00132; gatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
FT   ACT_SITE     85     85       Charge relay system (By similarity).
FT   ACT_SITE    160    160       Charge relay system (By similarity).
FT   ACT_SITE    184    184       Acyl-ester intermediate (By similarity).
SQ   SEQUENCE   513 AA;  54170 MW;  E4044181FF149693 CRC64;
     MSNETATLVK LSAAEQAAAV KKGDVTSREL VEAHLKVIEA AEPSIKAFLK VSGDVALEQA
     DAFDAKSAED KAALPELAGV PIAIKDMIVT KGIETTAASK ILEGWVPPYD ATVIEKLKAA
     GMPILGKTNL DEFAQGSSTE HSAYQTTHNP WDTERVPGGS GGGSASAVAA FEAPIALGTD
     TGGSIRQPGA LTGTVGVKPT YGGVSRFGAI AMASSLDQIG PVSRTVLDSA LLQEIIGGHD
     KRDSTSIPEG PRPMVAAARE GAKRDLKGMK VGLIKELGGD GFQPGVEARF NEAVDKLKEM
     GAEVVEVSVP HIGYSLGAYY IIMPSEVSSN LARYDGMRYG LRVMPPTGVP QTAANMMAYT
     REAGFGDEVK RRIILGTYAL SAGYYDAWYG SAQKVRTLII EDFKKAFEQV DVLVAPTSPS
     TAFKFGEKMD DPLAMYMNDI ATIPANLAGV PAMSIPAGLS DDGLPVGFQF IAPQQRDEVM
     YKPAAALEAA LEDSWNGPIW NDLKTPWLDG LGK
//
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