ID GATA_ROSCS Reviewed; 490 AA.
AC A7NKM0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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=Rcas_1951;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000804; ABU58040.1; -; Genomic_DNA.
DR RefSeq; WP_012120464.1; NC_009767.1.
DR AlphaFoldDB; A7NKM0; -.
DR SMR; A7NKM0; -.
DR STRING; 383372.Rcas_1951; -.
DR KEGG; rca:Rcas_1951; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_0; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000000263; 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 PIRSF; PIRSF001221; Amidase_fungi; 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..490
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000203044"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 490 AA; 52334 MW; AAE52AAEAB6F38A1 CRC64;
MTPLYQLTVA QAREMLARGE ISSLELTDAL LTRIAAVEPK VRAFLVVDAA GARAQARAAD
ARRAAGDASP LLGIPMGIKD VISTQGLRTT CASKMLENYT PVYDATAVAR LKAAGAVILG
KLNCDEFAMG SSTENSAFQQ TRNPWNLERV PGGSSGGSAA AVAAGEAPAA LGTDTGGSIR
QPAALCGITG LKPTYGRVSR YGLVAFASSL DQIGPMARTV RDCAIVLRVI AGADPFDATC
TDYPAPDYEA ALTGDIRGLR IGVPREYFVA GMQPDVEAAV RTAIEVLREQ GAEVCEISLP
HTPYALPVYY LIAPAEASAN LARFDGVRYG LRVPGESYFD ELERTRGAGF GPEVRRRIML
GTYALSAGYY DAYYKRAQQV RTLIRRDYQQ AFEQVDVIAA PTTPTVAFKI GAHTDDPLAM
YLEDVCTLPL NLAGLPGLVV PCGFAEGLPI GLQLIGRAFD EESLLRVGDA YQRVTDWHTR
MPEVREDGSA
//
