ID   GATA_STRCO              Reviewed;         497 AA.
AC   Q9Z580;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-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=SCO5499; ORFNames=SC8D9.11;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939124; CAB37575.1; -; Genomic_DNA.
DR   PIR; T35815; T35815.
DR   RefSeq; NP_629634.1; NC_003888.3.
DR   RefSeq; WP_003973499.1; NZ_VNID01000011.1.
DR   AlphaFoldDB; Q9Z580; -.
DR   SMR; Q9Z580; -.
DR   STRING; 100226.SCO5499; -.
DR   GeneID; 1100939; -.
DR   KEGG; sco:SCO5499; -.
DR   PATRIC; fig|100226.15.peg.5583; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_11; -.
DR   InParanoid; Q9Z580; -.
DR   OMA; EVSCPHF; -.
DR   PhylomeDB; Q9Z580; -.
DR   Proteomes; UP000001973; 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..497
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT                   /id="PRO_0000105210"
FT   ACT_SITE        80
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  52270 MW;  B5CD253F8AF6868E CRC64;
     MSDIIKLTAA EIAAKIASGE LTAVQVTEAH LARIEAVDEK VHAFLHVDRE GALAQARAVD
     EKRERGEKLG PLAGVPLALK DIFTTEGIPT TVGSKILEGW IPPYDATVTK RLKAADVVIL
     GKTNMDEFAM GSSTENSAYG PTGNPWDLTK IPGGSGGGSS AALAAFQAPL AIGTDTGGSI
     RQPASVTGTV GVKPTYGGVS RYGMVAFSSS LDQGGPCART VLDAALLHEV IAGHDPMDST
     SIDAPVPAVV EAARNGSVDG MRVGVVKQFR GEGYQAGVVQ RFDESVELLK SLGAEIVELD
     CPSFDLALSA YYLIAPSECS SNLARFDGLR YGARVGDDGT HSAEEVTSLT REAGFGPEVK
     RRIMLGTYAL SSGYYDAYYG SAQKVRTLIK QEFERAFEQV DVIVSPTTPT TAFAIGERAD
     DPMAMYLADL CTIPTNLAGN AAMSLPCGLA PEDNLPVGLQ IIAPAMKDDR LYKVGAAVEA
     AFVEKWGHPL IEEAPSL