ID A0A1J4WEU8_9BACT Unreviewed; 487 AA.
AC A0A1J4WEU8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 16.
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:OIO44863.1};
GN ORFNames=AUJ25_03280 {ECO:0000313|EMBL:OIO44863.1};
OS Parcubacteria group bacterium CG1_02_37_13.
OC Bacteria.
OX NCBI_TaxID=1805302 {ECO:0000313|EMBL:OIO44863.1, ECO:0000313|Proteomes:UP000182656};
RN [1] {ECO:0000313|EMBL:OIO44863.1, ECO:0000313|Proteomes:UP000182656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_37_13 {ECO:0000313|EMBL:OIO44863.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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|HAMAP-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|HAMAP-Rule:MF_00120}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OIO44863.1}.
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DR EMBL; MNWC01000049; OIO44863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4WEU8; -.
DR STRING; 1805302.AUJ25_03280; -.
DR Proteomes; UP000182656; 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; 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.
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:OIO44863.1}.
FT DOMAIN 24..474
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 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 487 AA; 53034 MW; 66534B919BB28AEE CRC64;
MIKDNFTIKK IQEGLKCKDF SAVELAKKYL KVIEEKDKDI HAFLEVSENM ALKQAQEVDE
KIAKQEKLTL LAGVPCSVKD AIMVEGLKCT AGSKMLKNYK AVYSATSVKK IVEQGALILG
KTNLDEFAMG SSTEHSAFGP TKNPWDLTRV PGGTSGGSVA SVSAGENIFS LGSDTGGSIR
QPASFCGVVG LKPTYGAVSR YGLIAHGSSL EQIGAIANNV EDCQTVFNTI KGKDEKDATS
VALSFPTTNL PTGRQVAGRT TNYKIGIPRE YFGEGLDEEV KESVLKAVKG LEEQGCQVKE
VSLPHAVYAL ACYYIISTSE ASANLARYDG VRYGHRAKSQ KQKANSLLED YIADRSEGFG
SEVKRRIILG TFCLSSGYYD AYYQKAQKVR ELIKQDFALA FEKVDLLITP TSPFCAFKLG
EKLDDPLQMY LADIYTVSIN LAGLPALSMP CGLNKEKLPI GLQIIGPHFT ENKIFDLAKK
TEITLEK
//
