ID GATA_FRATF Reviewed; 481 AA.
AC A7NEM1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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}; OrderedLocusNames=FTA_1949;
OS Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=458234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FTNF002-00 / FTA;
RX PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA Lion C., Dempsey M.P.;
RT "Complete genome sequence of Francisella tularensis subspecies holarctica
RT FTNF002-00.";
RL PLoS ONE 4:E7041-E7041(2009).
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; CP000803; ABU62424.1; -; Genomic_DNA.
DR RefSeq; WP_003017412.1; NC_009749.1.
DR AlphaFoldDB; A7NEM1; -.
DR SMR; A7NEM1; -.
DR KEGG; fta:FTA_1949; -.
DR HOGENOM; CLU_009600_0_3_6; -.
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.
FT CHAIN 1..481
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000015831"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 173
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 481 AA; 52396 MW; CDA715EBE4E4D709 CRC64;
MSYIKKLRAR LDSGEISAVE LTKEYLAKIK EQDKRINSII TLCEAEALKE AEDADAIISA
GKQGLLTGIP ILHKDLFCTK GIRTTAASKM LDNFVAPYDS TVTKNCKDQG MVTLGKLNMD
EFAMGSTNEY SYYGAVSNPW DLERVPGGSS GGSAAAVAAG FAPISTGSDT GGSVRQPASF
CGLTAMKPSY GSTSRFGMVA FASSFDQAGI FGHYAEDVAI MLDAIAGECE FDSTCVGVKQ
NHFTQDLEKD ISSKVIGVDE SLIKDLPAQI QEAVSKTLDN FKKLGAEIKS VKVPDLKEAL
STYYIITPAE AAANLARYDG IRYGYRNPEA RDLDELYRKS RTDGFGAEVK RRIMIGNYVL
ASSQYDSYYN KAQQLRKVMT DQINQIFTQV DAIFMPASPS EAFKKGDKLD PVSAYLSDIY
TIPANISGLP AIAFPIGFAN NLPVGGQLMA KAFNDNILTQ MVVQYQKHYG IEEFILQQAR
I
//
