ID   GATA_MYCPN              Reviewed;         478 AA.
AC   P75534;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=MPN_237; ORFNames=MP594;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00089; AAB96242.1; -; Genomic_DNA.
DR   PIR; S73920; S73920.
DR   RefSeq; NP_109925.1; NC_000912.1.
DR   RefSeq; WP_010874594.1; NC_000912.1.
DR   AlphaFoldDB; P75534; -.
DR   SMR; P75534; -.
DR   STRING; 272634.MPN_237; -.
DR   EnsemblBacteria; AAB96242; AAB96242; MPN_237.
DR   GeneID; 66609117; -.
DR   KEGG; mpn:MPN_237; -.
DR   PATRIC; fig|272634.6.peg.256; -.
DR   HOGENOM; CLU_009600_0_3_14; -.
DR   OMA; EVSCPHF; -.
DR   BioCyc; MPNE272634:G1GJ3-377-MON; -.
DR   Proteomes; UP000000808; 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..478
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105179"
FT   ACT_SITE        68
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  53230 MW;  F228E9AE4F641071 CRC64;
     MKSQILKLQQ TLTKKPASIN PLLQQIDGAI NEHWSSNFLL KNTVEWAQAQ APKNRSKSPL
     NNIPFVLKDN IATKGIVTTG GSRFLEDYIP PFSATVFELL NNSGALLVGK ANLDEFGLGG
     TGLHSGFGFV HHPWNETLIP GGSSSGSAYA VARGIVPFSI GTDTGDSVRR PASICNIVGF
     KPTYGLISRN GVYPYAPSLD HVGIFARYVY DVALVSDEII KHDKADFSAQ KSPDAGKFTR
     SLKESFNKQI KIGYLKPLEE WFDIELSKKW NSLKERITLE GCELIPFHFP LELLEVIDPV
     YKLISYSEAV SCYSNLTGIV FGQKLFEPNQ ASDFSKTITA NRDRFFGEQL KRRFIIGAFG
     TDKNNFTKYF EKAQKIRRVM VDAYLNLFKE ADFIVSPSAS GFTKTIAAVQ KGESFTNLVD
     DFLQLANFAG NPSITIPWLV KQKDQTIGLS VNANCFHDKQ LLQVAAWLEE LFQIEHDD