ID A0A0Q7C5A7_9ACTN Unreviewed; 512 AA.
AC A0A0Q7C5A7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ASC77_05615 {ECO:0000313|EMBL:KQW53737.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW53737.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW53737.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW53737.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW53737.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW53737.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQW53737.1}.
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DR EMBL; LMDV01000001; KQW53737.1; -; Genomic_DNA.
DR RefSeq; WP_056149579.1; NZ_LMDV01000001.1.
DR AlphaFoldDB; A0A0Q7C5A7; -.
DR STRING; 1736439.ASC77_05615; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000051939; 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:UP000051939};
KW Transferase {ECO:0000313|EMBL:KQW53737.1}.
FT DOMAIN 25..481
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 184
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 512 AA; 53039 MW; 19D088EC3D8935D0 CRC64;
MSGWIRKTAS EMADALAAGE VTSVELTQAH LDRIAAVDTP TDRRGVHAFL HVDAEGALAQ
AAESDARRSA GSPLSALDGV PIAVKDVLAT EGLPTTCGSK ILEGWIPPYD ATVVARLKAA
GLPILGKTNM DEFAMGSSTE HSAYGATHNP WDLDRIPGGS GGGSAAAVAA FEAPLAIGTD
TGGSIRQPGA VTGTVGVKPT YGGVSRYGLV ALANSLDQAG PVTRTVLDSA LLHEVIGGHD
PMDSTSIDQP LPDLVAAAKQ GAAGDLSGVR VGVIKELSGD GWQPGVITRF QESVDLLVKA
GAEVVEVSCP HFVHAMAAYY LILPAEASSN LAKFDAMRYG LRVWPEGKPD ASAEEVMRAT
RDAGFGDEVK RRIILGTYAL SSGYYDAYYG QAQKVRTLIS RDFEAAFEQA DVLVSPTAPT
TAFKLGEKLD DPIAMYLNDL ATIPANLAGV PGISVPSGLA EEDGLPAGFQ ILAPALADDR
CYRVGAALEA ALLEQWGGPL LDQAPALNGA DA
//
