ID   GATA_BORBU              Reviewed;         481 AA.
AC   O51317;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE            Short=Glu-ADT subunit A;
DE            EC=6.3.5.7;
GN   Name=gatA; OrderedLocusNames=BB_0342;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC       which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC       presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC       tRNA(Gln) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000783; AAC66715.2; -; Genomic_DNA.
DR   PIR; E70142; E70142.
DR   RefSeq; NP_212476.2; NC_001318.1.
DR   RefSeq; WP_010889731.1; NC_001318.1.
DR   AlphaFoldDB; O51317; -.
DR   SMR; O51317; -.
DR   STRING; 224326.BB_0342; -.
DR   PRIDE; O51317; -.
DR   EnsemblBacteria; AAC66715; AAC66715; BB_0342.
DR   KEGG; bbu:BB_0342; -.
DR   PATRIC; fig|224326.49.peg.738; -.
DR   HOGENOM; CLU_009600_0_3_12; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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; IPR036928; AS_sf.
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; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..481
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105141"
FT   ACT_SITE        78
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        153
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  53658 MW;  EB6FBE89905A7A81 CRC64;
     MDLSNLTLTK IQELVLTRKC KIYDILLAYK NNYELNKDIN GYIEFFDDSL EIAKRYDDCL
     KNCELEDLPL IGMLIAVKDN ISIQDKSLTC ASEILKGYIS PYDATVIKRL KNKGAILIGR
     TNMDEFAMGS TCEFSYYGAT LNPLNREYVI GGSSGGSAAV VAAFQAPFSL GSDTGGSVRL
     PASFSGILGF KPSYGGLSRY GLASYASSFD QIGFFSHSIE DIALILKHTC GSDKMDSTSV
     DIFDDFYPLK IESLQGKNLA VIKELSEDLM DKNVANSFAK FKLDLLSKGI NIKEVSIEEI
     NFILSIYYII SPVEASSNLA RYTGLCYGKR ISEGLSLNDF YFKHRSNFLS EEVKRRIVLG
     NYLLSERYDS KYYAKACEIL QNLIIPKFNK LFESCDFIIT PTSFVKPFRL GLDFDDPVKM
     YYSDICTVIA NLIGAPAISL PYSKDEEGLS IGMQIIGRSK KDFELLSFSK NVIRELGLNG
     I