ID E8MGJ7_BIFL2 Unreviewed; 513 AA.
AC E8MGJ7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 19.
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; RYDGVKY; -.
DR BioCyc; BLON565042:GIWN-230-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA: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; Amidase_sig_enz; 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
//
