GATA_BARBK
ID GATA_BARBK Reviewed; 494 AA.
AC A1UT20;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BARBAKC583_0835;
OS Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) 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; CP000524; ABM45182.1; -; Genomic_DNA.
DR RefSeq; WP_005767184.1; NC_008783.1.
DR AlphaFoldDB; A1UT20; -.
DR SMR; A1UT20; -.
DR STRING; 360095.BARBAKC583_0835; -.
DR EnsemblBacteria; ABM45182; ABM45182; BARBAKC583_0835.
DR KEGG; bbk:BARBAKC583_0835; -.
DR PATRIC; fig|360095.6.peg.811; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1239251at2; -.
DR Proteomes; UP000000643; 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; -; 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;
KW Reference proteome.
FT CHAIN 1..494
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000015800"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 183
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 494 AA; 53521 MW; D0079D550C9D6178 CRC64;
MTDLTMLTIA QARDSLKKGD FKATELTEAY LQAIELANPI LNAYVAVTAE QAMRMAAESD
NRLAKGEAGI LEGIPLGIKD LFATYDVHTQ GCSYILDGFK PKYESTVTAN LWKDGAVMLG
KLNMDEFAMG SSNETSYYGP VINPWRKKGS DEKLVPGGSS GGSSAAVAAR LCVGATATDT
GGSIRQPAAF TGTVGIKPTY GRCSRWGTIA YASSLDQAGP IGRDVRDCAI MLRSMASFDR
KDSTSVDLPI PDYEKCIGQS IKGMKIGIPK EYRLEWMSTE VIELWQKGMD FLKEAGAEIV
DISLPHVKYA LPSYYIVASA EASSNLARYD GVRFGLRMPG KDIVEMYEKT RSAGFGDEVK
QRILIGTYVL SSGYYDAYYI KAQKVRTLIK NDFDQCFAIG VDAILTPVTP TPAFGLADEK
IKNDSIAMYL NDIFTVPVNM VGLPGVSVPA GLSSSGLPLG LQLIGKPFAE EVILQIAYII
EQAAGTFSAK KWWP