ID A0A8A7L4B2_BRAHO Unreviewed; 482 AA. AC A0A8A7L4B2; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000256|HAMAP-Rule:MF_00120}; DE Short=Glu-ADT subunit A {ECO:0000256|HAMAP-Rule:MF_00120}; DE EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_00120}; GN Name=gatA {ECO:0000256|HAMAP-Rule:MF_00120, GN ECO:0000313|EMBL:QTM08052.1}; GN ORFNames=GQX60_03995 {ECO:0000313|EMBL:QTM08052.1}; OS Brachyspira hyodysenteriae (Treponema hyodysenteriae). OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=159 {ECO:0000313|EMBL:QTM08052.1}; RN [1] {ECO:0000313|EMBL:QTM08052.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BHZ375 {ECO:0000313|EMBL:QTM08052.1}; RA Garcia-Martin A.B., Schmitt S., Zeeh F., Perreten V.; RT "Complete genome sequences Brachyspira hyodysenteriae causing swine RT dysentery in Switzerland."; RL Submitted (DEC-2019) 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:0000256|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:0000256|ARBA:ARBA00001243, ECO:0000256|HAMAP- CC Rule:MF_00120}; CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP- CC Rule:MF_00120}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000256|ARBA:ARBA00008069, ECO:0000256|HAMAP-Rule:MF_00120}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP046930; QTM08052.1; -; Genomic_DNA. DR RefSeq; WP_047109778.1; NZ_JXNS01000062.1. DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:InterPro. 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00120}; Coiled coil {ECO:0000256|SAM:Coils}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00120}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00120}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00120}; Transferase {ECO:0000313|EMBL:QTM08052.1}. FT DOMAIN 39..468 FT /note="Amidase" FT /evidence="ECO:0000259|Pfam:PF01425" FT COILED 51..71 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 81 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120" FT ACT_SITE 156 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120" FT ACT_SITE 180 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120" SQ SEQUENCE 482 AA; 52767 MW; 0667CE13587BB90C CRC64; MELNELTIIQ IREKLKNKEI DAPTLVDSII KNIEEDNKRD DKIYAYLEIF KEEVLEQAKK AQERINNGED LPLLGVPLAI KDNLCYKDHL MTASSKMLEG YKAPYTAPTV QRLIDNGAII IGRTNMDEFA MGGTTETSNY GVTRNPKNRA HVPGGSSGGS AAAVAANFAF GALGSDTGGS IRQPASFCGI VGVKPTYGRV PRLGCIAMAS SLDQVGPLTK DVKDAALMTK IIAGFDPKES TTLNIPVPDY VAALDGNIKG MKIGLAKEYY DTDLIAADVK ENVMDAIGKL KDQGAEIVDI SLPNAKYGSR VYTAVMDVEV ASNMGRYDGI RYGYHPKGDF NLDEYYYTSR SVGLAFETRA RILFGTLMTG KRFFYSHYQH ALKVRKLMQM DFDNAFKNVD VIVSPTSPVT AGLLGTRDQT DSALSFLADS YVSNINLVGL PAMSVPCGVD KNNMPIGIQF ITKQFNEVDM FRMAYAHELA NK //