ID A0A0Q2XLY0_9RHOB Unreviewed; 493 AA.
AC A0A0Q2XLY0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:KQI67358.1};
GN ORFNames=AN189_15510 {ECO:0000313|EMBL:KQI67358.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI67358.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI67358.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI67358.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQI67358.1}.
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DR EMBL; LJAK01000013; KQI67358.1; -; Genomic_DNA.
DR RefSeq; WP_056037896.1; NZ_LJAK01000013.1.
DR AlphaFoldDB; A0A0Q2XLY0; -.
DR STRING; 1225657.AN189_15510; -.
DR PATRIC; fig|1225657.3.peg.3192; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000051463; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051463};
KW Transferase {ECO:0000313|EMBL:KQI67358.1}.
FT DOMAIN 25..473
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 78
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 493 AA; 52337 MW; 38066FB4339FCD4D CRC64;
MSDLTKLTIA AARDALRKGE VTSVELTSAC LTAIDAADTL NAFVHKTPEV AESQAKSADQ
RIQAGEAPDL CGIPLGIKDL FCTKGVASQA ASRILEGFKP EYESTVTTQL FDAGAVMLGK
LNMDEFAMGS SNETSVYGDA VNPWKVDDRQ LTPGGSSGGS AAAVAADLCL GATGTDTGGS
IRQPAAFTGI TGIKPTYGRV SRWGVVAFAS SLDQAGPMTK DVRDSAIMLQ AMSGFDAKDS
TSANIPVPDF EAALTGDIRG KVIGIPKEYR MDGMPAEIQK LWEDGTAMLR DAGAEVRDIS
LPHTKYALPA YYVIAPAEAS SNLARYDGVR FGHRAKLDAG DGITEMYEKT RAEGFGAEVQ
RRVMVGTYVL SAGFYDAYYN RARRVRALIK RDFDQVFADG VDAILTPATP SAAFGLGEMK
NADPIQMYLN DVFTVTVNLA GLPGISVPAG LDAKGLPLGL QLIGRPWEEG DLLNVAYALE
RSAGFNAKPA KWW
//
