GATA_MYCBT
ID GATA_MYCBT Reviewed; 494 AA.
AC C1AGC7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=JTY_3028;
OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=561275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL Vaccine 27:1710-1716(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; AP010918; BAH27306.1; -; Genomic_DNA.
DR RefSeq; WP_010950812.1; NZ_CP014566.1.
DR AlphaFoldDB; C1AGC7; -.
DR SMR; C1AGC7; -.
DR KEGG; mbt:JTY_3028; -.
DR HOGENOM; CLU_009600_0_3_11; -.
DR OMA; EVSCPHF; -.
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.
FT CHAIN 1..494
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000122485"
FT ACT_SITE 81
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 180
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 494 AA; 51436 MW; FE9F74EAAE74CE4A CRC64;
MTDIIRSDAA TLAAKIAIKE VSSTEITRAC LDQIEATDET YHAFLHVAAD EALAAAAAVD
KQVAAGEPLP SALAGVPLAL KDVFTTSDMP TTCGSKILEG WRSPYDATLT ARLRAAGIPI
LGKTNMDEFA MGSSTENSAY GPTRNPWNLD RVPGGSGGGS AAALAAFQAP LAIGSDTGGS
IRQPAALTAT VGVKPTYGTV SRYGLVACAS SLDQGGPCAR TVLDTALLHQ VIAGHDPRDS
TSVDAEVPDV VGAARAGAVG DLRGVRVGVV RQLHGGEGYQ PGVLASFEAA VEQLTALGAE
VSEVDCPHFD HALAAYYLIL PSEVSSNLAR FDAMRYGLRV GDDGTRSAEE VMAMTRAAGF
GPEVKRRIMI GTYALSAGYY DAYYNQAQKV RTLIARDLDA AYRSVDVLVS PTTPTTAFRL
GEKVDDPLAM YLFDLCTLPL NLAGHCGMSV PSGLSPDDGL PVGLQIMAPA LADDRLYRVG
AAYEAARGPL LSAI