ID   GATA_PROMP              Reviewed;         484 AA.
AC   Q7V1D0;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JAN-2019, entry version 86.
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=PMM0946;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P.,
RA   Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R.,
RA   Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M.,
RA   Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A.,
RA   Webb E.A., Zinser E.R., Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic
RT   niche differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in
CC       organisms which lack glutaminyl-tRNA synthetase. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + 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;
CC         EC=6.3.5.7; 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; BX548174; CAE19405.1; -; Genomic_DNA.
DR   RefSeq; WP_011132579.1; NC_005072.1.
DR   ProteinModelPortal; Q7V1D0; -.
DR   SMR; Q7V1D0; -.
DR   STRING; 59919.PMM0946; -.
DR   PRIDE; Q7V1D0; -.
DR   EnsemblBacteria; CAE19405; CAE19405; PMM0946.
DR   KEGG; pmm:PMM0946; -.
DR   eggNOG; ENOG4105C3P; Bacteria.
DR   eggNOG; COG0154; LUCA.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   OMA; MYLSDIF; -.
DR   OrthoDB; 1239251at2; -.
DR   BioCyc; PMAR59919:TX50_RS05040-MONOMER; -.
DR   Proteomes; UP000001026; Chromosome.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0004040; F:amidase activity; 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; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    484       Glutamyl-tRNA(Gln) amidotransferase
FT                                subunit A.
FT                                /FTId=PRO_0000105188.
FT   ACT_SITE     74     74       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    149    149       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    173    173       Acyl-ester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00120}.
SQ   SEQUENCE   484 AA;  52186 MW;  1A473E5882F6FE6F CRC64;
     MNFNSFRKEI YSGNASVKEL VNEFFLKIDS LNPKINAYTC LTKKIANSQS ENIDKLITNN
     QKLPSLAGIP IAIKDNICTK GVVTSCSSKM LKDFVSPYES SASGKLWSLG GICLGKTNLD
     EFAMGSSTET SVFGTTSNPW DVNRVPGGSS GGSAASVAAG LCLAAIGSDT GGSIRQPASF
     CGVVGLKPTY GRVSRWGLIA FASSLDQIGP ITNTVSDAAE ILYSISGKDN LDSTCLDKPV
     PNYLSDLDKS IKGIKIGIIE ECFDHPGLDP EVKESVLSSV ERFRSLGAEI HDIKCPRFND
     GIATYYVIAP CEASANLARY DGVKYGYRSE GESNLLEMIC KSRAEGFGDE VQRRILIGTY
     ALSAGYSDAY YKKAQRVRTL IRSDFDNAFN EVDVLLTPTC PTTAFLKGDF VNDPLSMYLS
     DLLTVPVNLA GLPAISIPCG FDKKGLPIGL QLIGNVLEEH RILNVANIFE KDAEVMNTKP
     NIEI
//