ID A0A1R1C9T2_9BACL Unreviewed; 485 AA.
AC A0A1R1C9T2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:OMF18797.1};
GN ORFNames=BK127_10145 {ECO:0000313|EMBL:OMF18797.1};
OS Paenibacillus sp. FSL H7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF18797.1, ECO:0000313|Proteomes:UP000187480};
RN [1] {ECO:0000313|EMBL:OMF18797.1, ECO:0000313|Proteomes:UP000187480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF18797.1,
RC ECO:0000313|Proteomes:UP000187480};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-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|ARBA:ARBA00025295, ECO:0000256|HAMAP-
CC 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:OMF18797.1}.
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DR EMBL; MRTH01000005; OMF18797.1; -; Genomic_DNA.
DR RefSeq; WP_076229913.1; NZ_MRTH01000005.1.
DR AlphaFoldDB; A0A1R1C9T2; -.
DR STRING; 1920421.BK127_10145; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000187480; 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:UP000187480};
KW Transferase {ECO:0000313|EMBL:OMF18797.1}.
FT DOMAIN 24..466
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 485 AA; 52338 MW; EBEA54659139A61C CRC64;
MSLFDLKLQE IHTQLKAKQI TVSDLVNESY TRIGQVDGKV KAFLKLDEEN ARTTAATLDE
QLDKSECRGL LFGLPIGIKD NIVTEGVTTT CASQFLRNFN PVYDATVVSK LKDAQAVSIG
KLNMDEFAMG GSNENSSFQI TYNPWNTEYV PGGSSGGSAA AVAAGEVYFS LGSDTGGSIR
QPAAYCGIVG LKPTYGLVSR FGLVAFASSL DQIGPLTKNV EDSAYLLQTI AGHDPKDSTS
ANVDIPDYIS ALSGDVKGLR IALPKEYMGE GIDPAVRESV LSALKVLEGL GAVVEEVSLP
HSEYAVATYY LLASSEASSN LARFDGVRYG VRADNPKNLL DLYHRSRSEG FGPEVKRRIM
LGTYALSSGY YDAYYLKAQK VRTLIKQDFD NVFENYDVVI GPTAPTTAFK VGSQVNDPLT
MYLNDILTIP VNLAGVPAIS VPCGFADGLP IGLQIIGKAL SEATILRVAY AFEQHTDFHK
QRPQL
//
