GATA_TREPS
ID GATA_TREPS Reviewed; 506 AA.
AC B2S4Q7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=TPASS_1020;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD71436.1; -; Genomic_DNA.
DR RefSeq; WP_010882464.1; NC_021508.1.
DR AlphaFoldDB; B2S4Q7; -.
DR SMR; B2S4Q7; -.
DR PRIDE; B2S4Q7; -.
DR EnsemblBacteria; ACD71436; ACD71436; TPASS_1020.
DR KEGG; tpp:TPASS_1020; -.
DR PATRIC; fig|455434.6.peg.1009; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000001202; 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.
FT CHAIN 1..506
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000095177"
FT REGION 153..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 196
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 506 AA; 54102 MW; F12BF02DB47FE3CC CRC64;
MDAHAITCAS WNMLKAQLEA GAISSLQIVR AFRNVYEEDT RSASPLGALV EFFSDAEEHA
RTADNLRASC AQSTKTAGAN GGSVSGKPLL GLPFAVKDNI SVKGKHCTCG SKLLADYRAP
YDATVVARLR AAGAIPLGRT NMDEFAMGSS TEYSVYGPTR NPRDRSRTSG GSSGGSAAAV
AGGQAPFALG TETGGSVRLP AAYCGLYGLK PTYGLLSRYG VVAFGSSLDQ IGFFATCIDD
IALALSVTSG KDLYDSTSTC PPPATGRHAV SHHLAPFSAH ECSILRAAVP RELVDAPGVH
PDVSAQFQRF LTWLRAQNVQ VEEVTLPALQ AAVPVYYLVA TAEAASNLAR FDGIRYGQRG
DTDALLENYY RAVRTSGFGP EVQRRIIVGN YVLSRHFSGD YYRTSVRVRS RIEQECTQLL
CSYHFIVCPT AATGAFPLGE RIHDPLAMYC SDLFTTFVNL ARLPALSVPV GTSGTGLPIG
IQIIGSQWQE CAVLRLAKRW EEAPHV
