ID GATA_EHRCR Reviewed; 487 AA.
AC Q2GGC5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=ECH_0703;
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000236; ABD44527.1; -; Genomic_DNA.
DR RefSeq; WP_006009841.1; NC_007799.1.
DR AlphaFoldDB; Q2GGC5; -.
DR SMR; Q2GGC5; -.
DR STRING; 205920.ECH_0703; -.
DR KEGG; ech:ECH_0703; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000008320; 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; 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;
KW Reference proteome.
FT CHAIN 1..487
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000241099"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 182
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 487 AA; 53160 MW; 9B37B09C16DE7D69 CRC64;
MKNILKLSIA EMHDNLKKRE FSAVELTKLH IEAVNNEKLN AFITKTPEIA LSAAEKADYI
FTHQKENLTP LTGIPVGIKD LFCTKHVRTT ACSNILKNFT PQYDSTVTKR LLDNGAVMLG
KLNMDEFAMG SSNSNSCFGH VKNPWVRADG VEVVPGGSSG GSSAAVAGFL CAGALGSDTG
GSVRQPAALC GIVGLKPTYG RCSRFGMIAF ASSLDQAGVL TRTVEDASLM LQSICGYDIQ
DSTSANIAVP KFSESITHTI KGKRIGIPKE YELSGKYQEY TEVSEMWAKG IQYLKDEGAE
IIEISLPHTS YALPVYYIIC SAEASSNLAR YDGIRYGARI SSDDINEMYE LTRGHNFGTE
VKRRILIGAY VLSSGYYDAY YNKAQRIRHL VINDFVESFK KIDYILTPTT PKEAFAINEQ
LDTLTMYLND VFTVPASLAG LPAISVPIGL SKSNLPLSLQ VIGNYYDEGG ILNVASIIEK
HTGKILK
//
