ID A0A1C2FX86_9GAMM Unreviewed; 481 AA.
AC A0A1C2FX86;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=A9R16_05605 {ECO:0000313|EMBL:OCX43820.1};
OS Acidiferrobacter thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Acidiferrobacter.
OX NCBI_TaxID=163359 {ECO:0000313|EMBL:OCX43820.1};
RN [1] {ECO:0000313|EMBL:OCX43820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZJ {ECO:0000313|EMBL:OCX43820.1};
RA Ma L.;
RT "Draft Genome Sequence of Acidiferrobacter thiooxydans ZJ, a Distinctive
RT Species of Ectothiorhodospiraceae.";
RL Submitted (AUG-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 -!- 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:OCX43820.1}.
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DR EMBL; MDCF01000252; OCX43820.1; -; Genomic_DNA.
DR RefSeq; WP_065972320.1; NZ_CP080624.1.
DR AlphaFoldDB; A0A1C2FX86; -.
DR STRING; 163359.A9R16_05605; -.
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:OCX43820.1}.
FT DOMAIN 21..461
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 173
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 481 AA; 51316 MW; C6F302F4EBB114EC CRC64;
MTLTITKIAE DLAAGRCSSR ELVDDALARI KTHAALNTFI TLDEEAARRD AEAADRARRA
GGRGMLAGVP IAHKDIFCTA GVKTTCASRM LADFVPPYDA TVVRKMKAAG CIMVGKTNMD
EFAMGSSNET SYFGPVRNPW DRERVPGGSS GGSAAAVAAR LVPAATGTDT GGSIRQPAAL
CGITGLKPSY GRVSRYGLIA FASSLDQAGP MAQTAEDCAH LLTAMAGFDE RDATSLDVPV
PDYAAELGKD LKGLRIGVVA EHFAEGIEPG VAEVVREALR EYERQGARLV DVSLPNSAHA
VPCYYVLAPA EASSNLARYD GVRYGYRVPE YQDLEDMYKK TRSQGFGSEV KRRIMVGTYA
LSAGYYDAYY VKALKLRRLI ADDFARAFAQ CDILAGPVSP STAFALGAKN TDPVSMYLND
IFTIPVNLAG LPALSLPAGF AGGLPVGLQL IGRYLDEARL LNAAHRFQQA TDWHARVPAG
I
//
