ID   GATA_TROWT              Reviewed;         524 AA.
AC   Q83GA1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120};
GN   OrderedLocusNames=TWT_412;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC   Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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). {ECO:0000255|HAMAP-Rule:MF_00120}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00120}.
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DR   EMBL; AE014184; AAO44509.1; -; Genomic_DNA.
DR   RefSeq; WP_011102561.1; NC_004572.3.
DR   AlphaFoldDB; Q83GA1; -.
DR   SMR; Q83GA1; -.
DR   STRING; 203267.TWT_412; -.
DR   KEGG; twh:TWT_412; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_11; -.
DR   OrthoDB; 9811471at2; -.
DR   Proteomes; UP000002200; 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; Amidase signature (AS) domain; 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   NCBIfam; TIGR00132; gatA; 1.
DR   PANTHER; PTHR11895:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 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..524
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105226"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        184
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT   ACT_SITE        208
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   524 AA;  56455 MW;  925927E8D616705A CRC64;
     MIRRAPFLIL LRFCRMGKMA CSGYPPFQGR IVLSEMPAHR LAALIRSKEV SALEVAESFI
     DNIEASDSRI CAFLYTDFSY TRDVARRVDE ELKSATKLSP LAGVPIAVKD MILTRDMPTT
     AGSKILEGWI PPYNATVIER ISRARMPILG KTNQDEFGMG SSTEYSAYKT TRNPWDLSRT
     AGGSGGGSSA AVSASQAPLA LGTDTGGSIR LPAHCTGTVG IRPTYGSVSR YGVIALASSF
     DQVGPCSSNI LDAALLHEVI AGYDPADAVS IKDQDLNFSQ AAYEGANRGI SGVRLGFVNP
     SNWCNSKITD LFGRTLKSLE SEGAVLHEVQ FPNFDHAVQA YYLIMQAEAS SNLSRYDSIR
     FGPQEMAASA SGTVSKTRSI RFGPEVKRRI LLGTHILSAG YYDDFYMSAQ KIRLLVKRDF
     AKIFSLVDVL LLPTAPTPAF KLGEKIDHHT SMYKSDTATT PASLAGLPAG SIPMGVIDGL
     PVGLQIIAPG QFDSRVYSTG AAIEQIIGDI HAMKNTKHNT GQTA
//