ID A0A1A2NCD6_9MYCO Unreviewed; 493 AA.
AC A0A1A2NCD6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=A5695_16005 {ECO:0000313|EMBL:OBH12695.1};
OS Mycobacterium sp. E1747.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH12695.1, ECO:0000313|Proteomes:UP000092218};
RN [1] {ECO:0000313|Proteomes:UP000092218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-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:OBH12695.1}.
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DR EMBL; LZJI01000047; OBH12695.1; -; Genomic_DNA.
DR RefSeq; WP_068078696.1; NZ_LZJI01000047.1.
DR AlphaFoldDB; A0A1A2NCD6; -.
DR STRING; 1834128.A5695_16005; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000092218; 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:OBH12695.1}.
FT DOMAIN 25..475
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
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 493 AA; 51303 MW; 5820571E3FF7976E CRC64;
MNEIIRSDAA TLAARIAARE LSSVEVTRAC LDQISATDDR YHAFLHVATD EALAAAAAID
EAVAAGEPLP SPLAGVPLAL KDVFTTVDMP TTCGSKILEG WRSPYDATVT TRLRAAGIPI
LGKTNMDEFA MGSSTENSAY GPTRNPWNLD RVPGGSGGGS AAALAAFQAP LAIGSDTGGS
IRQPAALTAT VGVKPTYGTV SRYGLVACAS SLDQGGPCAR TVLDTALLHH VIAGHDARDS
TSVEAAIPDV VGAAKAGAAG DLRGVRVGVV QQLRGDGYQP GVLSSFEAAV GRLTELGAEV
TEVDCPHFEY ALAAYYLILP SEVSSNLARF DAMRYGLRVG DDGTHSAEEV MALTRAAGFG
PEVKRRIMIG TYALSAGYYD AYYNQAQKVR TLIARDLDRA YESADVVVSP ATPTTAFPLG
EKVDDPLAMY LFDLCTLPLN LAGHCGMSVP AGLSPDDGLP VGLQIMAPAL ADDRLYRVGA
AYEVARGPLP SAI
//
