ID A0A1N7RJD1_9BURK Unreviewed; 500 AA.
AC A0A1N7RJD1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:SIT35164.1};
GN ORFNames=BN2476_20058 {ECO:0000313|EMBL:SIT35164.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT35164.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT35164.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT35164.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; CYGY02000002; SIT35164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7RJD1; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000195569; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 SUPFAM; SSF75304; Amidase signature (AS) enzymes; 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};
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:SIT35164.1}.
FT DOMAIN 22..480
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 174
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 500 AA; 53413 MW; E8E009EBE0F5AE07 CRC64;
MHEKSLTELR AALDAKQCSA VELAQTYLKR IADHGALNAF VHVDEQQTLA QAQAADAQLA
AGNAGPLTGL PIAHKDVFVT RNWRSTAGSK MLENYVSPFD ATVVERLARA GMVCVGKTNM
DEFAMGSSNE NSHFGPVQNP WDRKAVPGGS SGGSAAAVAA RLAPAATGTD TGGSIRQPAS
FSGITGIKPT YGRVSRYGMI AFASSLDQGG PMAHTATDCA LLLNAMAGFD ERDSTSLTHD
HEDYTRYLGQ AWSGANNSGD AAGKPLAGLR IGLPKEYFGA GLADDVRASI DAALKQYEAL
GATLVEVSLP KTELSIPVYY VIAPAEASSN LSRFDGVRYG HRAAEYRDLL DMYKKSRAEG
FGPEVKRRIL VGTYVLSHGY YDAYYLQAQK IRRIIAQDFQ EAFRKCDVIM GPVAPSVAWD
IGAKGDDPVQ MYLADIYTLS VSLAGLPGMS VPCGFGAGAN AQRPVGLQII GNYFNEARML
QVADAFQRVT DWHRKAPAGV
//
