ID   GATA_MYCGE              Reviewed;         477 AA.
AC   P47345;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=MG099;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
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; L43967; AAC71317.1; -; Genomic_DNA.
DR   PIR; I64210; I64210.
DR   RefSeq; WP_010869331.1; NC_000908.2.
DR   AlphaFoldDB; P47345; -.
DR   SMR; P47345; -.
DR   STRING; 243273.MG_099; -.
DR   EnsemblBacteria; AAC71317; AAC71317; MG_099.
DR   KEGG; mge:MG_099; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_7_6_14; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1239251at2; -.
DR   BioCyc; MGEN243273:G1GJ2-111-MON; -.
DR   Proteomes; UP000000807; 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..477
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105178"
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   477 AA;  53408 MW;  0D4A99D75C3DBF2B CRC64;
     MRSNILSLRA ILDKKPSAIN DVLTSINAKI ELNKSSNFLL KNTVEIYSKK INKSDEKILL
     NNIPYVLKDN IATKDIVTTG GSLFLKNYLP PFSATVFELL EMNGALLVGK ANMDEFGLGG
     TGSYSAFGVV HHPENSSLIA GGSSSGSAYA VAKDIVPFSI ATDTGDSIRR PASICNVVGF
     KPTYGLISRN GVFPYAPSMD HVGIFAKFVS DIAIVSDVVI KHDKTDFSSQ KSPDENQFFN
     ELAIPFTRSI RFGYLKPLEK LFNKHLQKKW NNLKKTLEQK NYQLIPLDFD VELLKVIDSI
     YKIISYSEAV SCYSNLTGIV FGQKVFEPNS PSNFDQTITR NRDQFLGKQL KRRFVIGAFA
     TDEKNFEKYF EKAQKIRRVL VDNFLNLFSD VDFVLSPSAS CFASTIEDIQ ANKPYTNIID
     DFLQLANFAG SPSITIPWLV QTKDQTIGLS ISANCFEDKK LLQIAYWFEQ LFDLNHD